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6T5X

Crystal structure of Salmonella typhimurium FabG in complex with NADPH at 1.5 A 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
A0046872molecular_functionmetal ion binding
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
B0046872molecular_functionmetal ion binding
B0050661molecular_functionNADP binding
B0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues35
Detailsbinding site for residue NDP A 301
ChainResidue
AGLY12
AALA87
AGLY88
AILE89
AILE136
AGLY137
ASER138
ATYR151
ALYS155
APRO181
AGLY182
ASER14
AILE184
ATHR186
AMET188
ATHR189
AHOH404
AHOH405
AHOH409
AHOH423
AHOH427
AHOH429
AARG15
AHOH434
AHOH450
AHOH453
AHOH454
AHOH463
AHOH491
AILE17
ATHR37
ALEU58
AASN59
AVAL60
AASN86

site_idAC2
Number of Residues6
Detailsbinding site for residue NA A 302
ChainResidue
AGLU233
ATHR234
AHOH452
BGLU233
BTHR234
BHOH532

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL A 303
ChainResidue
AARG91
AHOH409
AHOH423
AHOH428
AHOH542

site_idAC4
Number of Residues5
Detailsbinding site for residue GOL A 304
ChainResidue
ASER2
AASP225
AGLU226
AHOH403
AHOH433

site_idAC5
Number of Residues33
Detailsbinding site for residue NDP B 301
ChainResidue
BGLY12
BSER14
BARG15
BALA36
BTHR37
BLEU58
BASN59
BVAL60
BASN86
BALA87
BGLY88
BILE89
BILE136
BGLY137
BTYR151
BLYS155
BPRO181
BGLY182
BILE184
BTHR186
BHOH407
BHOH413
BHOH429
BHOH436
BHOH443
BHOH444
BHOH465
BHOH470
BHOH492
BHOH510
BHOH536
BHOH543
BHOH580

site_idAC6
Number of Residues6
Detailsbinding site for residue GOL B 302
ChainResidue
BILE89
BARG91
BARG123
BHOH405
BHOH409
BHOH444

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SvvgtmgnagQanYAAAKAGLiGFSkSLA
ChainResidueDetails
ASER138-ALA166

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10001
ChainResidueDetails
ATYR151
BTYR151

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLY12
AILE184
AGLU233
ATHR234
BGLY12
BTHR37
BGLY50
BGLY53
BASN59
BASN86
BSER138
ATHR37
BASN145
BTYR151
BILE184
BGLU233
BTHR234
AGLY50
AGLY53
AASN59
AASN86
ASER138
AASN145
ATYR151

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PDB entries from 2024-09-18

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