Structure of PDB 5dbv Chain A

Receptor sequence
>5dbvA (length=431) Species: 357809 (Lachnoclostridium phytofermentans ISDg) [Search protein sequence]
LGVFDDMNQAIEAAKEAQLVVKKMSMDQREKIISAIRKKTIEHAETLARM
AVEETGMGNVGHKILKHQLVAEKTPGTEDITTTAWSGDRGLTLVEMGPFG
VIGAITPCTNPSETIICNTIGMLAGGNTVVFNPHPAAIKTSNFAVQLINE
ASLSAGGPVNIACSVRKPTLDSSKIMMSHQDIPLIAATGGPGVVTAVLQS
GKRGIGAGAGNPPVLVDETADIRKAAEDIINGCTFDNNLPAIAEKEVVAI
DAIANELMNYMVKEQGCYAITKEQQEKLTNLVITPKGLNRNCVGKDARTL
LGMIGIDNIRCIIFEGEKEHPLISEELMMPILGIVRAKSFDDAVEKAVWL
EHGNRHSAHIHSKNVDRITTYAKAIDTAILVKNAPSYAAIGFGGEGFCTF
TIASRTGEGLTSASTFTKRRRCVMSDSLCIR
3D structure
PDB5dbv Insight into Coenzyme A cofactor binding and the mechanism of acyl-transfer in an acylating aldehyde dehydrogenase from Clostridium phytofermentans.
ChainA
Resolution1.77 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T137 G236 A269
Catalytic site (residue number reindexed from 1) T109 G208 A241
Enzyme Commision number ?
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 COA A I133 C136 N160 P161 H162 G217 G218 V221 A269 K273 R318 E357 M359 I105 C108 N132 P133 H134 G189 G190 V193 A241 K245 R290 E326 M328
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0008774 acetaldehyde dehydrogenase (acetylating) activity
GO:0016491 oxidoreductase activity
GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor

View graph for
Molecular Function
External links
PDB RCSB:5dbv, PDBe:5dbv, PDBj:5dbv
PDBsum5dbv
PubMed26899032
UniProtA9KN57

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