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4BO6

Crystal structure of 3-oxoacyl-(acyl-carrier-protein) reductase (FabG) from Pseudomonas aeruginosa in complex with 2,3-dihydroindol-1-yl-(2- thiophen-3-yl-1,3-thiazol-4-yl)methanone at 2.8A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004316molecular_function3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
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
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
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
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 Residues9
DetailsBINDING SITE FOR RESIDUE 36P A 1248
ChainResidue
APHE107
AVAL110
AASN111
ALEU114
AGLY163
APHE164
BASN111
BLEU114
BPHE164

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 36P C 1248
ChainResidue
CVAL110
CASN111
CLEU114
CGLY163
CPHE164
DTRP106
DASN111
DLEU114
DPHE164

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
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10001
ChainResidueDetails
ATYR154
BTYR154
CTYR154
DTYR154

site_idSWS_FT_FI2
Number of Residues28
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLY12
BASP62
BASN89
BSER141
BTYR154
BILE187
CGLY12
CTHR37
CASP62
CASN89
CSER141
ATHR37
CTYR154
CILE187
DGLY12
DTHR37
DASP62
DASN89
DSER141
DTYR154
DILE187
AASP62
AASN89
ASER141
ATYR154
AILE187
BGLY12
BTHR37

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PDB entries from 2024-12-25

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