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4K6C

X-ray crystal structure of a putative Acetoacyl-CoA reductase from Burkholderia cenocepacia

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005737cellular_componentcytoplasm
A0016491molecular_functionoxidoreductase activity
A0018454molecular_functionacetoacetyl-CoA reductase activity
A0042619biological_processpoly-hydroxybutyrate biosynthetic process
B0000166molecular_functionnucleotide binding
B0005737cellular_componentcytoplasm
B0016491molecular_functionoxidoreductase activity
B0018454molecular_functionacetoacetyl-CoA reductase activity
B0042619biological_processpoly-hydroxybutyrate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 301
ChainResidue
ASER35
AASN38
AHOH579

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 302
ChainResidue
AHOH541
AHOH582
AHOH583

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO B 301
ChainResidue
BPRO59
BSER67

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SvngskgsvgQtnYAAAKAGMhGFTkSLA
ChainResidueDetails
ASER140-ALA168

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PDB entries from 2024-11-06

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