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3EZL

Crystal Structure of Acetoacetyl-CoA Reductase from Burkholderia Pseudomallei 1710b

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005737cellular_componentcytoplasm
A0016491molecular_functionoxidoreductase activity
A0018454molecular_functionacetoacetyl-CoA reductase activity
A0032787biological_processmonocarboxylic acid metabolic process
A0042619biological_processpoly-hydroxybutyrate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE P4C A 249
ChainResidue
ATYR9
AALA91
ATHR113
AHOH344
AGLY12
AGLY35
ACYS36
AGLY62
AASN63
AVAL64
ATHR70
APHE74

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SvngqkgqfgQtnYSTAKAGIhGFTmSLA
ChainResidueDetails
ASER142-ALA170

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
ATYR155
ASER142
AASN114
ALYS159

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
AGLN152
ALYS159

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
ATYR155
ALYS159

246905

PDB entries from 2025-12-31

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