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3OID

Crystal Structure of Enoyl-ACP Reductases III (FabL) from B. subtilis (complex with NADP and TCL)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004318molecular_functionenoyl-[acyl-carrier-protein] reductase (NADH) 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
A0141148molecular_functionenoyl-[acyl-carrier-protein] reductase (NADPH) activity
B0004318molecular_functionenoyl-[acyl-carrier-protein] reductase (NADH) 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
B0141148molecular_functionenoyl-[acyl-carrier-protein] reductase (NADPH) activity
C0004318molecular_functionenoyl-[acyl-carrier-protein] reductase (NADH) 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
C0141148molecular_functionenoyl-[acyl-carrier-protein] reductase (NADPH) activity
D0004318molecular_functionenoyl-[acyl-carrier-protein] reductase (NADH) 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
D0141148molecular_functionenoyl-[acyl-carrier-protein] reductase (NADPH) activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TCL A 601
ChainResidue
AALA91
ASER92
AGLY93
ATYR151
AALA191
ALEU192
AHIS194
APHE195
ANDP501

site_idAC2
Number of Residues34
DetailsBINDING SITE FOR RESIDUE NDP A 501
ChainResidue
AGLY11
ASER13
AARG14
AGLY15
AVAL16
AASN34
ATYR35
AALA36
AARG37
ASER38
AALA61
AASN62
AVAL63
AASN89
AALA90
AALA91
AILE112
AILE139
ASER140
ASER141
ALYS158
AGLY184
AGLY185
AALA186
AILE187
ATHR189
AALA191
ALEU192
AHOH270
AHOH287
AHOH316
AHOH325
AHOH478
ATCL601

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TCL B 603
ChainResidue
BSER92
BGLY93
BTYR151
BALA191
BLEU192
BHIS194
BPHE195
BNDP503

site_idAC4
Number of Residues34
DetailsBINDING SITE FOR RESIDUE NDP B 503
ChainResidue
BGLY11
BSER13
BARG14
BGLY15
BVAL16
BASN34
BALA36
BARG37
BSER38
BALA61
BASN62
BVAL63
BASN89
BALA90
BALA91
BILE112
BILE139
BSER140
BSER141
BLYS158
BGLY184
BGLY185
BALA186
BILE187
BTHR189
BALA191
BHOH263
BHOH278
BHOH293
BHOH442
BHOH443
BHOH446
BHOH548
BTCL603

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TCL C 604
ChainResidue
CALA91
CSER92
CGLY93
CTYR151
CALA191
CHIS194
CPHE195
CNDP504

site_idAC6
Number of Residues33
DetailsBINDING SITE FOR RESIDUE NDP C 504
ChainResidue
CALA36
CARG37
CSER38
CALA61
CASN62
CVAL63
CASN89
CALA90
CALA91
CILE112
CILE139
CSER140
CSER141
CLYS158
CGLY184
CGLY185
CALA186
CILE187
CTHR189
CALA191
CHOH261
CHOH281
CHOH379
CHOH380
CHOH381
CHOH432
CTCL604
CGLY11
CSER13
CARG14
CGLY15
CVAL16
CASN34

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE TCL D 602
ChainResidue
DSER92
DGLY93
DTYR151
DALA191
DLEU192
DPHE195
DNDP502

site_idAC8
Number of Residues34
DetailsBINDING SITE FOR RESIDUE NDP D 502
ChainResidue
DGLY11
DSER13
DARG14
DGLY15
DVAL16
DASN34
DALA36
DARG37
DSER38
DALA61
DASN62
DVAL63
DASN89
DALA90
DALA91
DILE112
DILE139
DSER140
DSER141
DLYS158
DGLY184
DGLY185
DALA186
DILE187
DTHR189
DALA191
DHOH262
DHOH288
DHOH305
DHOH326
DHOH327
DHOH328
DHOH329
DTCL602

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:21185310
ChainResidueDetails
ATYR151
ALYS158
BTYR151
BLYS158
CTYR151
CLYS158
DTYR151
DLYS158

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:21185310, ECO:0007744|PDB:3OID
ChainResidueDetails
ASER13
BASN89
BLYS158
BILE187
CSER13
CALA36
CASN62
CASN89
CLYS158
CILE187
DSER13
AALA36
DALA36
DASN62
DASN89
DLYS158
DILE187
AASN62
AASN89
ALYS158
AILE187
BSER13
BALA36
BASN62

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PDB entries from 2024-07-24

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