Local view for "http://wifo5-04.informatik.uni-mannheim.de/drugbank/resource/drugs/DB04456"
| Predicate | Value (sorted: none) |
|---|---|
| drugbank:description |
"
experimental
This compound belongs to the metalloid oxides. These are inorganic compounds containing an oxygen atom of an oxidation state of -2, in which the heaviest atom bonded to the oxygen is a metalloid.
Metalloid Oxides
Inorganic Compounds
Mixed Metal/Non-metal Compounds
Metalloid Organides
Metalloid Oxides
logP
-0.86
ChemAxon
IUPAC Name
arsorous acid
ChemAxon
Traditional IUPAC Name
trihydroxyarsenite(iii)
ChemAxon
Molecular Weight
125.9436
ChemAxon
Monoisotopic Weight
125.929815379
ChemAxon
SMILES
O[As](O)O
ChemAxon
Molecular Formula
AsH3O3
ChemAxon
InChI
InChI=1S/AsH3O3/c2-1(3)4/h2-4H
ChemAxon
InChIKey
InChIKey=GCPXMJHSNVMWNM-UHFFFAOYSA-N
ChemAxon
Polar Surface Area (PSA)
60.69
ChemAxon
Refractivity
7.69
ChemAxon
Polarizability
6.27
ChemAxon
Rotatable Bond Count
0
ChemAxon
H Bond Acceptor Count
3
ChemAxon
H Bond Donor Count
3
ChemAxon
pKa (strongest acidic)
6.84
ChemAxon
pKa (strongest basic)
-6.2
ChemAxon
Physiological Charge
-1
ChemAxon
Number of Rings
0
ChemAxon
Bioavailability
1
ChemAxon
Rule of Five
true
ChemAxon
ChEBI
49900
PubChem Compound
545
PubChem Substance
46508436
ChemSpider
530
PDB
TAS
BE0001885
Arsenical pump-driving ATPase
Escherichia coli
# 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
Arsenical pump-driving ATPase
Inorganic ion transport and metabolism
Anion-transporting ATPase. Catalyzes the extrusion of the oxyanions arsenite, antimonite and arsenate. Maintenance of a low intracellular concentration of oxyanion produces resistance to the toxic agents
arsA
Cytoplasmic
None
5.64
63189.0
Escherichia coli
GenBank Gene Database
J02591
GenBank Protein Database
151857
UniProtKB
P08690
UniProt Accession
ARSA1_ECOLX
Arsenical resistance ATPase
Arsenite-translocating ATPase
Arsenite-transporting ATPase
EC 3.6.3.16
>Arsenical pump-driving ATPase
MQFLQNIPPYLFFTGKGGVGKTSISCATAIRLAEQGKRVLLVSTDPASNVGQVFSQTIGI
TIQAIASVPGLSALEIDPQAAAQQYRARIVDPIKGVLPDDVVSSINEQLSGACTTEIAAF
DEFTGLLTDASLLTRFDHIIFDTAPTGHTIRLLQLPGAWSSFIDSNPEGASCLGPMAGLE
KQREQYAYAVEALSDPKRTRLVLVARLQKSTLQEVARTHLELAAIGLKNQYLVINGVLPK
TEAANDTLAAAIWEREQEALANLPADLAGLPTDTLFLQPVNMVGVSALSRLLSTQPVASP
SSDEYLQQRPDIPSLSALVDDIARNEHGLIMLMGKGGVGKTTMAAAIAVRLADMGFDVHL
TTSDPAAHLSMTLNGSLNNLQVSRIDPHEETERYRQHVLETKGKELDEAGKRLLEEDLRS
PCTEEIAVFQAFSRVIREAGKRFVVMDTAPTGHTLLLLDATGAYHREIAKKMGEKGHFTT
PMMLLQDPERTKVLLVTLPETTPVLEAANLQADLERAGIHPWGWIINNSLSIADTRSPLL
RMRAQQELPQIESVKRQHASRVALVPVLASEPTGIDKLKQLAG
>1752 bp
ATGCAATTCTTACAGAATATCCCCCCTTATCTGTTTTTTACGGGTAAAGGAGGCGTGGGT
AAAACCTCTATTTCCTGCGCCACGGCGATCCGTCTGGCAGAACAGGGGAAACGGGTGCTG
CTGGTCAGTACCGATCCGGCCTCAAACGTAGGCCAGGTGTTTAGCCAGACGATTGGCATT
ACCATTCAGGCAATAGCCTCTGTTCCTGGATTGTCGGCTCTTGAGATTGATCCTCAGGCT
GCTGCACAACAGTACCGGGCCAGAATCGTTGACCCTATTAAAGGCGTCCTGCCTGATGAC
GTTGTTTCCAGCATCAACGAACAACTGTCAGGTGCATGCACAACAGAGATTGCGGCTTTT
GATGAATTTACCGGATTACTGACAGATGCCTCTCTGCTGACGCGGTTTGACCATATCATT
TTTGATACCGCGCCGACGGGTCACACCATTCGCCTTCTGCAGTTGCCGGGCGCCTGGAGT
AGCTTTATTGACAGCAATCCCGAGGGCGCGTCCTGTCTCGGCCCAATGGCGGGGCTGGAA
AAGCAGCGTGAACAGTATGCCTATGCTGTTGAAGCGTTGTCTGATCCAAAGCGTACCCGA
CTGGTATTAGTTGCTCGTCTGCAAAAATCCACGTTGCAGGAAGTCGCCCGGACTCATCTG
GAACTTGCCGCCATCGGCCTTAAAAATCAGTACCTGGTTATTAATGGCGTTCTGCCCAAA
ACTGAAGCGGCAAACGATACACTGGCTGCTGCAATATGGGAGCGTGAACAGGAGGCGCTG
GCCAATCTTCCCGCTGATCTTGCAGGTTTGCCAACTGACACATTATTTCTCCAGCCGGTC
AATATGGTCGGTGTGTCTGCGCTCAGCAGGCTTCTCTCCACTCAGCCTGTAGCGTCGCCA
TCCTCGGATGAATACCTGCAACAGCGGCCTGATATTCCGTCACTTTCTGCGTTGGTTGAT
GATATTGCCCGTAATGAACATGGCCTGATTATGCTGATGGGTAAAGGTGGCGTGGGGAAA
ACCACGATGGCTGCTGCCATTGCTGTCAGGCTGGCCGACATGGGATTTGATGTCCATCTG
ACAACATCTGATCCTGCGGCGCATCTCAGCATGACCCTGAACGGTAGCCTTAACAACCTG
CAGGTCAGCAGGATCGATCCTCACGAGGAAACGGAACGCTATCGTCAGCATGTTCTTGAA
ACAAAGGGAAAAGAACTGGACGAAGCGGGAAAACGCCTGCTGGAAGAGGACTTACGCTCA
CCTTGCACTGAGGAAATTGCTGTTTTCCAGGCCTTTTCACGGGTGATTCGTGAAGCGGGT
AAACGTTTCGTGGTGATGGATACGGCTCCGACCGGACACACGCTGTTGCTGCTGGATGCT
ACAGGCGCGTACCACCGCGAAATTGCGAAGAAAATGGGAGAAAAAGGCCATTTCACCACA
CCGATGATGCTGCTTCAGGATCCGGAGCGCACTAAAGTGTTACTGGTCACGCTGCCGGAA
ACCACGCCCGTGCTTGAAGCGGCAAATTTACAGGCCGACCTTGAGCGTGCAGGCATTCAC
CCCTGGGGCTGGATTATCAATAACAGCCTTTCCATTGCGGATACCCGTTCGCCACTGCTT
CGTATGCGGGCACAACAGGAACTTCCGCAGATAGAGAGCGTTAAACGCCAGCACGCCAGC
CGTGTCGCTCTTGTTCCCGTACTGGCGTCAGAACCAACCGGCATCGACAAACTCAAACAA
CTTGCTGGGTAA
PF02374
ArsA_ATPase
component
membrane
component
cell
function
binding
function
ATP binding
function
catalytic activity
function
hydrolase activity, acting on acid anhydrides
function
hydrolase activity
function
hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
function
nucleotide binding
function
pyrophosphatase activity
function
purine nucleotide binding
function
nucleoside-triphosphatase activity
function
adenyl nucleotide binding
process
ion transport
process
physiological process
process
cellular physiological process
process
anion transport
process
transport
BE0001321
Arsenate reductase
Escherichia coli
# 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
Arsenate reductase
Inorganic ion transport and metabolism
Reduction of arsenate [As(V)] to arsenite [As(III)]. This protein expands the substrate specificity of arsAB pump which can extrude arsenite and antimonite to allow for arsenate pumping and resistance
arsC
None
4.99
15831.0
Escherichia coli
GenBank Gene Database
J02591
GenBank Protein Database
151859
UniProtKB
P08692
UniProt Accession
ARSC1_ECOLX
Arsenical pump modifier
EC 1.20.4.1
>Arsenate reductase
MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLR
KNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQ
KGAFTKEDGEKVVDEAGKRLK
>426 bp
ATGAGCAACATCACTATTTATCATAACCCAGCCTGCGGCACCTCGCGTAATACGCTGGAG
ATGATCCGCAACAGCGGTACCGAGCCGACCATTATTCTTTACCTTGAAAACCCGCCTTCG
AGGGATGAGCTGGTTAAACTTATTGCCGATATGGGTATTTCAGTACGAGCGCTGCTGCGT
AAAAACGTTGAACCTTACGAGCAACTGGGTCTTGCAGAAGATAAATTTACTGACGATCAG
CTCATCGACTTTATGTTGCAACACCCAATTCTGATTAACCGTCCGATCGTGGTTACGCCG
CTGGGAACCAGACTGTGCCGTCCTTCTGAAGTGGTTCTGGATATCCTACAGGATGCGCAG
AAAGGGGCTTTCACTAAGGAAGACGGTGAAAAAGTCGTTGATGAAGCAGGAAAACGGCTG
AAATAA
PF03960
ArsC
function
catalytic activity
function
oxidoreductase activity
function
arsenate reductase activity
function
arsenate reductase (glutaredoxin) activity
process
physiological process
process
metabolism
process
cellular metabolism
process
generation of precursor metabolites and energy
process
electron transport
"
|
| rdfs:label |
"Trihydroxyarsenite(Iii)"
|
| rdf:type | |
| owl:sameAs |
All properties reside in the graph file:///home/swish/src/ClioPatria/guidelines3/drugbank_small.nt
The resource does not appear as an object