Structure of PDB 2fzw Chain A Binding Site BS03

Receptor Information
>2fzw Chain A (length=373) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ANEVIKCKAAVAWEAGKPLSIEEIEVAPPKAHEVRIKIIATAVCHTDAYT
LSGADPEGCFPVILGHLGAGIVESVGEGVTKLKAGDTVIPLYIPQCGECK
FCLNPKTNLCQKIRVTQGKGLMPDGTSRFTCKGKTILHYMGTSTFSEYTV
VADISVAKIDPLAPLDKVCLLGCGISTGYGAAVNTAKLEPGSVCAVFGLG
GVGLAVIMGCKVAGASRIIGVDINKDKFARAKEFGATECINPQDFSKPIQ
EVLIEMTDGGVDYSFECIGNVKVMRAALEACHKGWGVSVVVGVAASGEEI
ATRPFQLVTGRTWKGTAFGGWKSVESVPKLVSEYMSKKIKVDEFVTHNLS
FDEINKAFELMHSGKSIRTVVKI
Ligand information
Ligand IDPO4
InChIInChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
InChIKeyNBIIXXVUZAFLBC-UHFFFAOYSA-K
SMILES
SoftwareSMILES
CACTVS 3.341[O-][P]([O-])([O-])=O
ACDLabs 10.04[O-]P([O-])([O-])=O
OpenEye OEToolkits 1.5.0[O-]P(=O)([O-])[O-]
FormulaO4 P
NamePHOSPHATE ION
ChEMBL
DrugBankDB14523
ZINC
PDB chain2fzw Chain A Residue 1803 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB2fzw Structure-function relationships in human glutathione-dependent formaldehyde dehydrogenase. Role of Glu-67 and Arg-368 in the catalytic mechanism.
Resolution1.84 Å
Binding residue
(original residue number in PDB)		K83 K158
Binding residue
(residue number reindexed from 1)		K83 K158
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) C44 H45 T46 Y49 H66 L67 C96 C99 C102 C110 R114 C173 T177 R368
Catalytic site (residue number reindexed from 1) C44 H45 T46 Y49 H66 L67 C96 C99 C102 C110 R114 C173 T177 R368
Enzyme Commision number 1.1.1.-
1.1.1.1: alcohol dehydrogenase.
1.1.1.284: S-(hydroxymethyl)glutathione dehydrogenase.
Gene Ontology
Molecular Function
GO:0004022 alcohol dehydrogenase (NAD+) activity
GO:0005504 fatty acid binding
GO:0008270 zinc ion binding
GO:0009055 electron transfer activity
GO:0016491 oxidoreductase activity
GO:0018467 formaldehyde dehydrogenase (NAD+) activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
GO:0051903 S-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity
GO:0080007 S-nitrosoglutathione reductase (NADH) activity
GO:0106321 S-(hydroxymethyl)glutathione dehydrogenase (NADP+) activity
GO:0106322 S-(hydroxymethyl)glutathione dehydrogenase (NAD+) activity
Biological Process
GO:0001523 retinoid metabolic process
GO:0003016 respiratory system process
GO:0006629 lipid metabolic process
GO:0010430 fatty acid omega-oxidation
GO:0032496 response to lipopolysaccharide
GO:0044281 small molecule metabolic process
GO:0045777 positive regulation of blood pressure
GO:0046294 formaldehyde catabolic process
GO:0051409 response to nitrosative stress
GO:0051775 response to redox state
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005829 cytosol
GO:0070062 extracellular exosome

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2fzw, PDBe:2fzw, PDBj:2fzw
PDBsum2fzw
PubMed16605250
UniProtP11766|ADHX_HUMAN Alcohol dehydrogenase class-3 (Gene Name=ADH5)

[Back to BioLiP]