Structure of PDB 4pze Chain G

Receptor sequence
>4pzeG (length=283) Species: 381666 (Cupriavidus necator H16) [Search protein sequence]
SIRTVGIVGAGTMGNGIAQACAVVGLNVVMVDISDAAVQKGVATVASSLD
RLIKKEKLTEADKASALARIKGSTSYDDLKATDIVIEAATENYDLKVKIL
KQIDGIVGENVIIASNTSSISITKLAAVTSRADRFIGMHFFNPVPVMALV
ELIRGLQTSDTTHAAVEALSKQLGKYPITVKNSPGFVVNRILCPMINEAF
CVLGEGLASPEEIDEGMKLGCNHPIGPLALADMIGLDTMLAVMEVLYTEF
ADPKYRPAMLMREMVAAGYLGRKTGRGVYVYSK
3D structure
PDB4pze Crystal structure and biochemical properties of the (S)-3-hydroxybutyryl-CoA dehydrogenase PaaH1 from Ralstonia eutropha
ChainG
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S119 H140 E152 N190
Catalytic site (residue number reindexed from 1) S118 H139 E151 N189
Enzyme Commision number 1.1.1.35: 3-hydroxyacyl-CoA 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 CAA G G221 C222 N223 G220 C221 N222
BS02 CAA G H140 F142 N190 H139 F141 N189
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003857 3-hydroxyacyl-CoA dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0070403 NAD+ binding
Biological Process
GO:0006631 fatty acid metabolic process
GO:0009056 catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4pze, PDBe:4pze, PDBj:4pze
PDBsum4pze
PubMed24792376
UniProtQ0KEY8

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