Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4BO3

Crystal structure of 3-oxoacyl-(acyl-carrier-protein) reductase (FabG) from Pseudomonas aeruginosa in complex with 2-(3-(trifluoromethyl) anilino)pyridine-3-sulfonamide at 2.5A resolution

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
C0004316molecular_function3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
C0006629biological_processlipid metabolic process
C0006631biological_processfatty acid metabolic process
C0006633biological_processfatty acid biosynthetic process
C0016491molecular_functionoxidoreductase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0030497biological_processfatty acid elongation
C0050661molecular_functionNADP binding
C0051287molecular_functionNAD binding
D0004316molecular_function3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
D0006629biological_processlipid metabolic process
D0006631biological_processfatty acid metabolic process
D0006633biological_processfatty acid biosynthetic process
D0016491molecular_functionoxidoreductase activity
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0030497biological_processfatty acid elongation
D0050661molecular_functionNADP binding
D0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE U98 A 1248
ChainResidue
ATRP106
BLEU114
BALA156
BGLY163
BPHE164
APHE107
AVAL110
AASN111
ALEU114
AALA156
AGLY160
APHE164
BVAL110

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE U98 C 1248
ChainResidue
CTRP106
CPHE107
CASN111
CLEU114
CALA156
CGLY160
CPHE164
DVAL110
DLEU114
DALA156
DGLY163
DPHE164

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NI B 1248
ChainResidue
BHIS75
BHIS79
DGLU55

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SvvgamgnagQtnYAAAKAGLeGFTrALA
ChainResidueDetails
ASER141-ALA169

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10001","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues48
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

PDB statisticsPDBj update infoContact PDBjnumon