Structure of PDB 1cdo Chain A

Receptor sequence
>1cdoA (length=374) Species: 8053 (Gadus morhua callarias) [Search protein sequence]
ATVGKVIKCKAAVAWEANKPLVIEEIEVDVPHANEIRIKIIATGVCHTDL
YHLFEGKHKDGFPVVLGHEGAGIVESVGPGVTEFQPGEKVIPLFISQCGE
CRFCQSPKTNQCVKGWANESPDVMSPKETRFTCKGRKVLQFLGTSTFSQY
TVVNQIAVAKIDPSAPLDTVCLLGCGVSTGFGAAVNTAKVEPGSTCAVFG
LGAVGLAAVMGCHSAGAKRIIAVDLNPDKFEKAKVFGATDFVNPNDHSEP
ISQVLSKMTNGGVDFSLECVGNVGVMRNALESCLKGWGVSVLVGWTDLHD
VATRPIQLIAGRTWKGSMFGGFKGKDGVPKMVKAYLDKKVKLDEFITHRM
PLESVNDAIDLMKHGKCIRTVLSL
3D structure
PDB1cdo Crystal structure of cod liver class I alcohol dehydrogenase: substrate pocket and structurally variable segments.
ChainA
Resolution2.05 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C46 H47 T48 Y51 H68 E69 C98 C101 C104 C112 W116 C175 T179 R369
Catalytic site (residue number reindexed from 1) C46 H47 T48 Y51 H68 E69 C98 C101 C104 C112 W116 C175 T179 R369
Enzyme Commision number 1.1.1.1: alcohol dehydrogenase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 ZN A C46 H68 C46 H68
BS02 ZN A C98 C104 C112 C98 C104 C112
BS03 NAD A C46 H47 T48 C175 T179 G202 V204 D224 L225 V270 G271 V293 W295 C46 H47 T48 C175 T179 G202 V204 D224 L225 V270 G271 V293 W295
Gene Ontology
Molecular Function
GO:0004022 alcohol dehydrogenase (NAD+) activity
GO:0008270 zinc ion binding
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0051903 S-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity
Biological Process
GO:0046294 formaldehyde catabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1cdo, PDBe:1cdo, PDBj:1cdo
PDBsum1cdo
PubMed8845755
UniProtP26325|ADH1_GADMC Alcohol dehydrogenase 1

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