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5END

Crystal structure of beta-ketoacyl-acyl carrier protein reductase (FabG)(Q152A) from Vibrio cholerae

Functional Information from GO Data
ChainGOidnamespacecontents
A0004316molecular_function3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0030497biological_processfatty acid elongation
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
B0004316molecular_function3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0006633biological_processfatty acid biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0030497biological_processfatty acid elongation
B0050661molecular_functionNADP binding
B0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue GOL B 301
ChainResidue
BASN63
BASN66

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10001
ChainResidueDetails
ATYR155
BTYR155

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLY16
BASN63
BASN90
BSER142
BTYR155
BILE188
ATHR41
AASN63
AASN90
ASER142
ATYR155
AILE188
BGLY16
BTHR41

237992

PDB entries from 2025-06-25

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