Local view for "http://wifo5-04.informatik.uni-mannheim.de/drugbank/resource/drugs/DB03382"
Predicate | Value (sorted: none) |
---|---|
rdf:type | |
rdfs:label |
"S-Oxy Cysteine"
|
owl:sameAs | |
drugbank:description |
"
experimental
This compound belongs to the alpha amino acids and derivatives. These are amino acids in which the amino group is attached to the carbon atom immediately adjacent to the carboxylate group (alpha carbon), or a derivative thereof.
Alpha Amino Acids and Derivatives
Organic Compounds
Organic Acids and Derivatives
Carboxylic Acids and Derivatives
Amino Acids, Peptides, and Analogues
Polyamines
Enolates
Carboxylic Acids
Monoalkylamines
carboxylic acid
enolate
polyamine
primary amine
amine
primary aliphatic amine
organonitrogen compound
logP
-3
ALOGPS
logS
0.54
ALOGPS
Water Solubility
4.70e+02 g/l
ALOGPS
logP
-3.2
ChemAxon
IUPAC Name
[(2R)-2-amino-2-carboxyethane]sulfinyl
ChemAxon
Traditional IUPAC Name
(2R)-2-amino-2-carboxyethanesulfinyl
ChemAxon
Molecular Weight
136.15
ChemAxon
Monoisotopic Weight
136.006838753
ChemAxon
SMILES
N[C@@H](C[S]=O)C(O)=O
ChemAxon
Molecular Formula
C3H6NO3S
ChemAxon
InChI
InChI=1S/C3H6NO3S/c4-2(1-8-7)3(5)6/h2H,1,4H2,(H,5,6)/t2-/m0/s1
ChemAxon
InChIKey
InChIKey=KLKIIDDWGJYRSN-REOHCLBHSA-N
ChemAxon
Polar Surface Area (PSA)
80.39
ChemAxon
Refractivity
28.88
ChemAxon
Polarizability
11.78
ChemAxon
Rotatable Bond Count
3
ChemAxon
H Bond Acceptor Count
4
ChemAxon
H Bond Donor Count
2
ChemAxon
pKa (strongest acidic)
1.42
ChemAxon
pKa (strongest basic)
8.38
ChemAxon
Physiological Charge
0
ChemAxon
Number of Rings
0
ChemAxon
Bioavailability
1
ChemAxon
Rule of Five
true
ChemAxon
PubChem Compound
46936656
PubChem Substance
46509121
ChemSpider
10752581
PDB
CSX
BE0001513
Aspartate 1-decarboxylase
Shigella flexneri
# Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284
# Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423
unknown
Aspartate 1-decarboxylase
Coenzyme transport and metabolism
L-aspartate = beta-alanine + CO(2)
panD
None
6.09
13834.0
Shigella flexneri
GenBank Gene Database
AE005674
GenBank Protein Database
24050337
UniProtKB
P0A793
UniProt Accession
PAND_SHIFL
Aspartate 1-decarboxylase precursor
Aspartate alpha- decarboxylase
EC 4.1.1.11
>Aspartate 1-decarboxylase precursor
MIRTMLQGKLHRVKVTHADLHYEGSCAIDQDFLDAAGILENEAIDIWNVTNGKRFSTYAI
AAERGSRIISVNGAAAHCASVGDIVIIASFVTMPDEEARTWRPNVAYFEGDNEMKRTAKA
IPVQVA
>369 bp
TCAAGCAACCTGTACCGGAATCGCTTTCGCGGTACGTTTCATTTCATTGTCGCCTTCAAA
ATAGGCGACATTGGGTCGCCAGGTGCGAGCTTCTTCATCTGGCATGGTAACGAAGCTGGC
GATGATGACAATATCGCCGACGCTGGCGCAGTGGGCCGCCGCACCGTTAACAGAAATAAT
TCTCGAACCGCGTTCTGCCGCGATGGCATAAGTGGAGAAACGCTTGCCGTTGGTGACATT
CCAGATATCGATGGCTTCGTTTTCGAGAATACCGGCTGCGTCAAGAAAATCCTGGTCAAT
GGCGCAAGAACCTTCATAGTGCAGGTCCGCATGAGTCACTTTCACGCGGTGGAGTTTGCC
CTGCAGCAT
PF02261
Asp_decarbox
function
carboxy-lyase activity
function
aspartate 1-decarboxylase activity
function
catalytic activity
function
lyase activity
function
carbon-carbon lyase activity
process
amino acid metabolism
process
amino acid and derivative metabolism
process
pyruvate family amino acid metabolism
process
alanine metabolism
process
physiological process
process
alanine biosynthesis
process
metabolism
process
cellular metabolism
BE0002148
Prolyl endopeptidase
Human
# Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284
# Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423
# Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235
unknown
Prolyl endopeptidase
Amino acid transport and metabolism
Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long
PREP
6q22
Cytoplasm
None
5.58
80764.0
Human
HUGO Gene Nomenclature Committee (HGNC)
HGNC:9358
GenAtlas
PREP
GeneCards
PREP
GenBank Gene Database
X74496
GenBank Protein Database
558596
UniProtKB
P48147
UniProt Accession
PPCE_HUMAN
EC 3.4.21.26
PE
Post-proline cleaving enzyme
>Prolyl endopeptidase
MLSFQYPDVYRDETAVQDYHGHKICDPYAWLEDPDSEQTKAFVEAQNKITVPFLEQCPIR
GLYKERMTELYDYPKYSCHFKKGKRYFYFYNTGLQNQRVLYVQDSLEGEARVFLDPNILS
DDGTVALRGYAFSEDGEYFAYGLSASGSDWVTIKFMKVDGAKELPDVLERVKFSCMAWTH
DGKGMFYNSYPQQDGKSDGTETSTNLHQKLYYHVLGTDQSEDILCAEFPDEPKWMGGAEL
SDDGRYVLLSIREGCDPVNRLWYCDLQQESSGIAGILKWVKLIDNFEGEYDYVTNEGTVF
TFKTNRQSPNYRVINIDFWDPEESKWKVLVPEHEKDVLEWIACVRSNFLVLCYLHDVKNI
LQLHDLTTGALLKTFPLDVGSIVGYSGQKKDTEIFYQFTSFLSPGIIYHCDLTKEELEPR
VFREVTVKGIDASDYQTVQIFYPSKDGTKIPMFIVHKKGIKLDGSHPAFLYGYGGFNISI
TPNYSVSRLIFVRHMGGILAVANIRGGGEYGETWHKGGILANKQNCFDDFQCAAEYLIKE
GYTSPKRLTINGGSNGGLLVAACANQRPDLFGCVIAQVGVMDMLKFHKYTIGHAWTTDYG
CSDSKQHFEWLVKYSPLHNVKLPEADDIQYPSMLLLTADHDDRVVPLHSLKFIATLQYIV
GRSRKQSNPLLIHVDTKAGHGAGKPTAKVIEEVSDMFAFIARCLNVDWIP
>2133 bp
ATGCTGTCCTTCCAGTACCCCGACGTGTACCGCGACGAGACCGCCGTACAGGATTATCAT
GGTCATAAAATTTGTGACCCTTACGCCTGGCTTGAAGACCCCGACAGTGAACAGACTAAG
GCCTTTGTGGAGGCCCAGAATAAGATTACTGTGCCATTTCTTGAGCAGTGTCCCATCAGA
GGTTTATACAAAGAGAGAATGACTGAACTATATGATTATCCCAAGTATAGTTGCCACTTC
AAGAAAGGAAAACGGTATTTTTATTTTTACAATACAGGTTTGCAGAACCAGCGAGTATTA
TATGTACAGGATTCCTTAGAGGGGGAGGCCAGAGTGTTCCTGGACCCCAACATACTGTCT
GACGATGGCACAGTGGCACTCCGAGGTTATGCGTTCAGCGAAGATGGTGAATATTTTGCC
TATGGTCTGAGTGCCAGTGGCTCAGACTGGGTGACAATCAAGTTCATGAAAGTTGATGGT
GCCAAAGAGCTTCCAGATGTGCTTGAAAGAGTCAAGTTCAGCTGTATGGCCTGGACCCAT
GATGGGAAGGGAATGTTCTACAACTCATACCCTCAACAGGATGGAAAAAGTGATGGCACA
GAGACATCTACCAATCTCCACCAAAAGCTCTACTACCATGTCTTGGGAACCGATCAGTCA
GAAGATATTTTGTGTGCTGAGTTTCCTGATGAACCTAAATGGATGGGTGGAGCTGAGTTA
TCTGATGATGGCCGCTATGTCTTGTTATCAATAAGGGAAGGATGTGATCCAGTAAACCGA
CTCTGGTACTGTGACCTACAGCAGGAATCCAGTGGCATCGCGGGAATCCTGAAGTGGGTA
AAACTGATTGACAACTTTGAAGGGGAATATGACTACGTGACCAATGAGGGGACGGTGTTC
ACATTCAAGACGAATCGCCAGTCTCCCAACTATCGCGTGATCAACATTGACTTCTGGGAT
CCTGAAGAGTCTAAGTGGAAAGTACTTGTTCCTGAGCATGAGAAAGATGTCTTAGAATGG
ATAGCTTGTGTCAGGTCCAACTTCTTGGTCTTATGCTACCTCCATGACGTCAAGAACATT
CTGCAGCTCCATGACCTGACTACTGGTGCTCTCCTTAAGACCTTCCCGCTCGATGTCGGC
AGCATTGTAGGGTACAGCGGTCAGAAGAAGGACACTGAAATCTTCTATCAGTTTACTTCC
TTTTTATCTCCAGGTATCATTTATCACTGTGATCTTACCAAAGAGGAGCTGGAGCCAAGA
GTTTTCCGAGAGGTGACCGTAAAAGGAATTGATGCTTCTGATTACCAGACAGTCCAGATT
TTCTACCCTAGCAAGGATGGTACGAAGATTCCAATGTTCATTGTGCATAAAAAAGGCATA
AAATTGGATGGCTCTCATCCAGCTTTCTTATATGGCTATGGCGGCTTCAACATATCCATC
ACACCCAACTACAGTGTTTCCAGGCTTATTTTTGTGAGACACATGGGTGGTATCCTGGCA
GTGGCCAACATCAGAGGAGGTGGCGAATATGGAGAGACGTGGCATAAAGGTGGTATCTTG
GCCAACAAACAAAACTGCTTTGATGACTTTCAGTGTGCTGCTGAGTATCTGATCAAGGAA
GGTTACACATCTCCCAAGAGGCTGACTATTAATGGAGGTTCAAATGGAGGCCTCTTAGTG
GCTGCTTGTGCAAATCAGAGACCTGACCTCTTTGGTTGTGTTATTGCCCAAGTTGGAGTA
ATGGACATGCTGAAGTTTCATAAATATACCATCGGCCATGCTTGGACCACTGATTATGGG
TGCTCGGACAGCAAACAACACTTTGAATGGCTTGTCAAATACTCTCCATTGCATAATGTG
AAGTTACCAGAAGCAGATGACATCCAGTACCCGTCCATGCTGCTCCTCACTGCTGACCAT
GATGACCGCGTGGTCCCGCTTCACTCCCTGAAGTTCATTGCCACCCTTCAGTACATCGTG
GGCCGCAGCAGGAAGCAAAGCAACCCCCTGCTTATCCACGTGGACACCAAGGCGGGCCAC
GGGGCGGGGAAGCCCACAGCCAAAGTGATAGAGGAAGTCTCAGACATGTTTGCGTTCATC
GCGCGGTGCCTGAATGTCGACTGGATTCCATAA
PF00326
Peptidase_S9
PF02897
Peptidase_S9_N
function
prolyl oligopeptidase activity
function
hydrolase activity
function
peptidase activity
function
endopeptidase activity
function
serine-type endopeptidase activity
function
serine-type peptidase activity
function
catalytic activity
process
metabolism
process
macromolecule metabolism
process
protein metabolism
process
cellular protein metabolism
process
proteolysis
process
physiological process
BE0003065
Exopolyphosphatase
Aquifex aeolicus (strain VF5)
unknown
Exopolyphosphatase
Nucleotide transport and metabolism
ppx
None
8.14
35497.0
Aquifex aeolicus (strain VF5)
GenBank Gene Database
AE000657
UniProtKB
O67040
UniProt Accession
O67040_AQUAE
>Exopolyphosphatase
MSLDNKPIMRVASIDIGSYSVRLTIAQIKDGKLSIILERGRITSLGTKVKETGRLQEDRI
EETIQVLKEYKKLIDEFKVERVKAVATEAIRRAKNAEEFLERVKREVGLVVEVITPEQEG
RYAYLAVAYSLKPEGEVCVVDQGGGSTEYVFGKGYKVREVISLPIGIVNLTETFFKQDPP
TEEEVKRFFEFLEKELSKVKKPVDTIVGLGGTITTLAALEYNVYPYDPQKVHGKVLTYGQ
IKKWFDTFKEIPSEERSKRFRQVEDRRAKVILAGIGIFLKTLEIFEKDCLIVSDWGLREG
VLVSEVLKENHS
>939 bp
TTAGGAATGATTTTCCTTTAATACTTCACTCACGAGAACGCCTTCTCTGAGTCCCCAGTC
GCTCACGATTAAACAATCCTTTTCAAAAATTTCTAAGGTTTTTAAGAATATGCCTATTCC
CGCGAGGATTACCTTTGCCCTCCTGTCCTCAACCTGCCTGAACCTCTTACTCCTTTCCTC
CGAAGGGATTTCTTTGAAAGTATCAAACCACTTCTTTATCTGTCCGTAAGTCAAAACTTT
TCCGTGAACTTTCTGTGGGTCGTAAGGGTAAACGTTATACTCAAGTGCCGCCAGAGTCGT
TATAGTTCCGCCCAGTCCCACAATCGTGTCAACAGGTTTCTTTACCTTACTAAGTTCCTT
CTCTAAAAATTCAAAAAATCTTTTGACTTCCTCTTCCGTTGGAGGGTCCTGCTTGAAGAA
GGTCTCGGTCAAGTTCACTATACCTATGGGTAGGGAAATTACTTCCCTCACTTTATACCC
CTTTCCGAAAACGTATTCCGTTGAACCACCCCCCTGGTCCACTACACAAACCTCTCCTTC
GGGCTTTAAAGAGTATGCAACCGCAAGGTAGGCATATCTCCCTTCCTGTTCGGGAGTAAT
CACTTCAACTACGAGTCCGACTTCTCTTTTTACCCTCTCCAGAAATTCCTCTGCGTTTTT
TGCCCTCCTTATTGCCTCCGTTGCTACGGCCTTTACCCGTTCTACCTTGAATTCATCAAT
TAACTTCTTATACTCCTTCAGCACCTGAATGGTTTCCTCTATCCTGTCCTCTTGAAGCCT
TCCCGTTTCCTTTACCTTTGTCCCGAGGGAGGTAATCCTTCCCCTCTCAAGGATTATGGA
GAGTTTTCCGTCTTTGATTTGGGCTATCGTTAGTCTCACGGAGTAGGAGCCTATGTCTAT
GGACGCCACCCTCATAATTGGTTTATTATCTAAAGACAT
PF02541
Ppx-GppA
BE0003066
Conserved protein
Mycobacterium tuberculosis
unknown
Conserved protein
Involved in FMN binding
Rv2991
None
6.52
18204.0
Mycobacterium tuberculosis
GenBank Gene Database
BX842581
UniProtKB
O53240
UniProt Accession
O53240_MYCTU
>Hypothetical protein
MGTKQRADIVMSEAEIADFVNSSRTGTLATIGPDGQPHLTAMWYAVIDGEIWLETKAKSQ
KAVNLRRDPRVSFLLEDGDTYDTLRGVSFEGVAEIVEEPEALHRVGVSVWERYTGPYTDE
CKPMVDQMMNKRVGVRIVARRTRSWDHRKLGLPHMSVGGSTAP
>492 bp
ATGGGAACCAAACAGCGCGCCGACATCGTCATGTCCGAGGCTGAAATCGCCGACTTCGTC
AACTCGAGCCGTACCGGAACGCTGGCCACCATCGGACCCGACGGCCAGCCGCACTTGACG
GCGATGTGGTATGCCGTGATCGACGGCGAAATCTGGCTGGAGACCAAGGCCAAGTCGCAG
AAGGCCGTCAACCTCCGACGGGATCCGCGGGTGAGCTTCCTGCTTGAAGACGGCGACACC
TACGACACGCTGCGCGGCGTGTCGTTCGAGGGCGTTGCCGAGATCGTCGAGGAGCCCGAG
GCGCTGCACCGCGTCGGGGTCAGCGTGTGGGAACGCTACACCGGCCCCTACACCGACGAG
TGCAAACCGATGGTCGACCAGATGATGAACAAGCGGGTCGGTGTGCGCATCGTGGCCCGT
CGGACCCGCTCGTGGGATCACCGCAAGCTGGGGCTGCCACACATGTCGGTGGGTGGCTCG
ACCGCCCCGTAG
PF01243
Pyridox_oxidase
function
FMN binding
function
oxidoreductase activity
function
oxidoreductase activity, acting on the CH-NH2 group of donors
function
binding
function
oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
function
pyridoxamine-phosphate oxidase activity
function
catalytic activity
function
nucleotide binding
process
vitamin metabolism
process
water-soluble vitamin metabolism
process
physiological process
process
vitamin B6 metabolism
process
metabolism
process
pyridoxine metabolism
process
cellular metabolism
process
pyridoxine biosynthesis
BE0003067
Probable thiol peroxidase
Mycobacterium tuberculosis
unknown
Probable thiol peroxidase
Involved in oxidoreductase activity
Has antioxidant activity. Could remove peroxides or H(2)O(2) (By similarity)
tpx
None
4.12
16896.0
Mycobacterium tuberculosis
GenBank Gene Database
BX842578
UniProtKB
P66952
UniProt Accession
TPX_MYCTU
EC 1.11.1.-
>Probable thiol peroxidase
MAQITLRGNAINTVGELPAVGSPAPAFTLTGGDLGVISSDQFRGKSVLLNIFPSVDTPVC
ATSVRTFDERAAASGATVLCVSKDLPFAQKRFCGAEGTENVMPASAFRDSFGEDYGVTIA
DGPMAGLLARAIVVIGADGNVAYTELVPEIAQEPNYEAALAALGA
>498 bp
ATGGCACAGATAACCCTGCGAGGAAACGCGATCAATACCGTCGGTGAGCTACCTGCTGTC
GGATCCCCGGCCCCGGCCTTCACCCTGACCGGGGGCGATCTGGGGGTGATCAGCAGCGAC
CAGTTCCGGGGTAAGTCCGTGTTGCTGAACATCTTTCCATCCGTGGACACACCGGTGTGC
GCGACGAGTGTGCGAACCTTCGACGAGCGTGCGGCGGCAAGTGGCGCTACCGTGCTGTGT
GTCTCGAAGGATCTGCCGTTCGCCCAGAAGCGCTTCTGCGGCGCCGAGGGCACCGAAAAC
GTCATGCCCGCGTCGGCATTCCGGGACAGCTTCGGCGAGGATTACGGCGTGACCATCGCC
GACGGGCCGATGGCCGGGCTGCTCGCCCGCGCAATCGTGGTGATCGGCGCGGACGGCAAC
GTCGCCTACACGGAATTGGTGCCGGAAATCGCGCAAGAACCCAACTACGAAGCGGCGCTG
GCCGCGCTGGGCGCCTAG
PF08534
Redoxin
function
thiol peroxidase activity
function
antioxidant activity
function
peroxidase activity
BE0002390
Superoxide dismutase [Cu-Zn]
Human
# Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235
unknown
Superoxide dismutase [Cu-Zn]
Involved in copper, zinc superoxide dismutase activity
Destroys radicals which are normally produced within the cells and which are toxic to biological systems
SOD1
Cytoplasm
None
6.07
15936.0
Human
HUGO Gene Nomenclature Committee (HGNC)
HGNC:11179
GenAtlas
SOD1
GeneCards
SOD1
GenBank Gene Database
L44139
UniProtKB
P00441
UniProt Accession
SODC_HUMAN
EC 1.15.1.1
>Superoxide dismutase [Cu-Zn]
MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTS
AGPHFNPLSRKHGGPKDEERHVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVV
HEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
>465 bp
ATGGCGACGAAGGCCGTGTGCGTGCTGAAGGGCGACGGCCCAGTGCAGGGCATCATCAAT
TTCGAGCAGAAGGAAAGTAATGGACCAGTGAAGGTGTGGGGAAGCATTAAAGGACTGACT
GAAGGCCTGCATGGATTCCATGTTCATGAGTTTGGAGATAATACAGCAGGCTGTACCAGT
GCAGGTCCTCACTTTAATCCTCTATCCAGAAAACACGGTGGGCCAAAGGATGAAGAGAGG
CATGTTGGAGACTTGGGCAATGTGACTGCTGACAAAGATGGTGTGGCCGATGTGTCTATT
GAAGGTTCTGTGATCTCACTCTCAGGAGACCATTGCATCATTGGCCGCACACTGGTGGTC
CATGAAAAAGCAGATGACTTGGGCAAAGGTGGAAATGAAGAAAGTACAAAGACAGGAAAC
GCTGGAAGTCGTTTGGCTTGTGGTGTAATTGGGATCGCCCAATAA
PF00080
Sod_Cu
function
oxidoreductase activity
function
ion binding
function
metal ion binding
function
oxidoreductase activity, acting on superoxide radicals as acceptor
function
binding
function
superoxide dismutase activity
function
copper, zinc superoxide dismutase activity
function
catalytic activity
process
oxygen and reactive oxygen species metabolism
process
superoxide metabolism
process
physiological process
process
metabolism
process
cellular metabolism
BE0002597
NADH peroxidase
Enterococcus faecalis (strain ATCC 700802 / V583)
unknown
NADH peroxidase
Involved in oxidoreductase activity
Peroxidase whose active site is a redox-active cysteine- sulfenic acid
npr
None
4.56
49566.0
Enterococcus faecalis (strain ATCC 700802 / V583)
GenBank Gene Database
X62755
UniProtKB
P37062
UniProt Accession
NAPE_ENTFA
EC 1.11.1.1
Npx
NPXase
>NADH peroxidase
MKVIVLGSSHGGYEAVEELLNLHPDAEIQWYEKGDFISFLSCGMQLYLEGKVKDVNSVRY
MTGEKMESRGVNVFSNTEITAIQPKEHQVTVKDLVSGEERVENYDKLIISPGAVPFELDI
PGKDLDNIYLMRGRQWAIKLKQKTVDPEVNNVVVIGSGYIGIEAAEAFAKAGKKVTVIDI
LDRPLGVYLDKEFTDVLTEEMEANNITIATGETVERYEGDGRVQKIVTDKNAYDADLVVV
AVGVRPNTAWLKGTLELHPNGLIKTDEYMRTSEPDVFAVGDATLIKYNPADTEVNIALAT
NARKQGRFAVKNLEEPVKPFPGVQGSSGLAVFDYKFASTGINEVMAQKLGKETKAVTVVE
DYLMDFNPDKQKAWFKLVYDPETTQILGAQLMSKADLTANINAISLAIQAKMTIEDLAYA
DFFFQPAFDKPWNIINTAALEAVKQER
>1344 bp
ATGAAAGTTATTGTTTTAGGATCATCACATGGAGGTTATGAAGCGGTAGAGGAATTACTA
AATCTTCATCCTGATGCAGAAATTCAATGGTATGAGAAAGGTGATTTTATCTCATTCTTG
TCTTGTGGCATGCAGTTGTACCTAGAAGGAAAAGTGAAAGATGTTAATTCTGTTCGCTAT
ATGACTGGCGAAAAAATGGAGAGCCGTGGTGTAAATGTCTTTTCTAATACTGAAATTACA
GCGATTCAACCAAAAGAACATCAAGTGACAGTGAAAGATTTAGTGTCAGGTGAAGAACGT
GTTGAAAATTATGATAAATTAATCATCAGTCCCGGAGCTGTCCCATTTGAATTAGATATT
CCAGGTAAAGATTTGGATAATATTTACTTGATGCGTGGTCGTCAATGGGCCATTAAATTA
AAACAAAAAACAGTAGATCCAGAAGTCAATAATGTGGTTGTGATTGGTAGTGGTTATATT
GGGATTGAAGCTGCCGAAGCATTTGCAAAAGCCGGTAAAAAGGTTACCGTTATTGATATT
TTAGATCGTCCATTAGGGGTGTATCTAGATAAAGAATTTACAGATGTTTTAACAGAAGAG
ATGGAAGCCAATAACATTACCATTGCAACTGGTGAAACAGTTGAACGTTACGAAGGCGAC
GGTCGTGTGCAAAAAGTCGTTACAGATAAAAATGCGTACGATGCTGATTTGGTCGTTGTA
GCGGTTGGTGTCCGTCCAAACACTGCTTGGTTAAAAGGTACCTTAGAATTACATCCGAAT
GGCCTAATCAAGACGGATGAATACATGCGGACAAGTGAGCCAGATGTATTTGCAGTAGGG
GATGCTACGTTAATTAAATACAATCCTGCAGACACAGAAGTAAATATTGCCTTAGCAACG
AATGCTCGTAAACAAGGTCGCTTTGCTGTGAAAAACCTAGAGGAACCAGTTAAACCTTTC
CCTGGTGTTCAAGGATCTTCTGGCTTGGCCGTCTTTGATTATAAATTTGCTTCAACAGGG
ATTAACGAAGTCATGGCTCAAAAATTAGGAAAAGAAACAAAAGCGGTGACAGTAGTAGAA
GACTACTTGATGGACTTTAATCCAGACAAACAAAAAGCTTGGTTTAAATTAGTGTATGAT
CCTGAAACAACACAAATTTTAGGCGCTCAATTAATGTCAAAAGCAGATTTAACTGCAAAC
ATTAATGCTATTTCATTAGCGATTCAAGCCAAAATGACAATTGAAGACTTAGCCTATGCG
GATTTCTTCTTCCAACCAGCGTTTGACAAACCTTGGAATATTATTAATACAGCGGCTTTA
GAAGCGGTGAAACAAGAACGTTAA
PF00070
Pyr_redox
PF07992
Pyr_redox_2
PF02852
Pyr_redox_dim
component
cell
component
intracellular
component
cytoplasm
function
disulfide oxidoreductase activity
function
catalytic activity
function
oxidoreductase activity
process
generation of precursor metabolites and energy
process
electron transport
process
physiological process
process
metabolism
process
cellular metabolism
"
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All properties reside in the graph file:///home/swish/src/ClioPatria/guidelines3/drugbank_small.nt
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