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3OSU

Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, FabG, from Staphylococcus aureus

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
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
B0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG A 247
ChainResidue
ATHR93
AGLN151
ATYR154
AHOH319
AHOH348

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG A 248
ChainResidue
APRO149
AGLY150
AHOH345

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG A 249
ChainResidue
AALA51
ALYS52
AHOH362
AGLU48

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG A 250
ChainResidue
AASN89
AALA90
AGLY91

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG A 251
ChainResidue
ALYS74
AGLN127
AHOH350

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG A 252
ChainResidue
AARG170
BVAL146
BASN148
BPHE186
BGLN206

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG A 253
ChainResidue
ALYS52
AGLY53
APEG254

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG A 254
ChainResidue
ALYS50
AGLY53
APEG253
BASP197
BLEU204

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG A 255
ChainResidue
AASN62
AALA64
AASP67
ATHR112

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A 256
ChainResidue
AARG14
ALYS41

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 257
ChainResidue
AASN89
ALYS158
AHOH298

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 258
ChainResidue
AGLN127
AARG130
AGLN131
BASP228
BLYS231

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 259
ChainResidue
ALYS5
AASP84
AGLY134
AALA226
AHOH290
AHOH292

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG B 247
ChainResidue
ALYS166
AHOH271
BHOH310
BHOH338

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG B 248
ChainResidue
AVAL146
AASN148
AGLN206
AMSE244
BARG170

site_idBC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG B 249
ChainResidue
BGLN127
BHOH320
BHOH331

site_idBC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG B 250
ChainResidue
BASN89
BALA90
BGLY91

site_idBC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PEG B 251
ChainResidue
BGLN151
BTYR154

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10001
ChainResidueDetails
ATYR154
BTYR154

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLY11
BSER141
BTYR154
BILE187
AASN62
AASN89
ASER141
ATYR154
AILE187
BGLY11
BASN62
BASN89

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PDB entries from 2024-04-24

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