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1SJD

x-ray structure of o-succinylbenzoate synthase complexed with n-succinyl phenylglycine

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0009234biological_processmenaquinone biosynthetic process
A0016829molecular_functionlyase activity
A0016853molecular_functionisomerase activity
A0043748molecular_functionO-succinylbenzoate synthase activity
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0009234biological_processmenaquinone biosynthetic process
B0016829molecular_functionlyase activity
B0016853molecular_functionisomerase activity
B0043748molecular_functionO-succinylbenzoate synthase activity
B0046872molecular_functionmetal ion binding
C0003824molecular_functioncatalytic activity
C0009234biological_processmenaquinone biosynthetic process
C0016829molecular_functionlyase activity
C0016853molecular_functionisomerase activity
C0043748molecular_functionO-succinylbenzoate synthase activity
C0046872molecular_functionmetal ion binding
D0003824molecular_functioncatalytic activity
D0009234biological_processmenaquinone biosynthetic process
D0016829molecular_functionlyase activity
D0016853molecular_functionisomerase activity
D0043748molecular_functionO-succinylbenzoate synthase activity
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE NPG A 1200
ChainResidue
AMET50
AASP316
APHE323
AHOH1201
AHOH1222
AHOH1303
AHOH1382
ASER135
ALYS161
ALYS163
AASN191
ALYS263
AGLY291
AMET292
AILE293

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE NPG B 1300
ChainResidue
BPHE23
BMET50
BSER135
BLYS163
BASN191
BLYS263
BGLY291
BMET292
BILE293
BASP316
BPHE323
BHOH1301
BHOH1330
BHOH1560
BHOH1561

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE NPG C 1400
ChainResidue
CMET50
CSER135
CLYS161
CLYS163
CASN191
CLYS263
CGLY291
CMET292
CILE293
CASP316
CPHE323
CHOH1401
CHOH1418
CHOH1468
CHOH1582

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE NPG D 1500
ChainResidue
DMET50
DSER135
DLYS161
DLYS163
DASN191
DASP239
DLYS263
DGLY291
DMET292
DILE293
DASP316
DPHE323

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE NPG B 1163
ChainResidue
AASP61
AGLY62
AHIS65
BASP61
BGLY62
BHIS65
BARG68
BHIS69
BHOH1341
BHOH1403
BHOH1657

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE NPG C 1164
ChainResidue
CASP61
CGLY62
CHIS65
CHOH1711
CHOH1728
DASP61
DGLY62
DHIS65
DHIS69
DHOH1547

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:14705949, ECO:0000305|PubMed:15134446
ChainResidueDetails
ALYS163
BLYS163
CLYS163
DLYS163

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:14705949, ECO:0000305|PubMed:15134446
ChainResidueDetails
ALYS263
BLYS263
CLYS263
DLYS263

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:15134446, ECO:0007744|PDB:1SJB
ChainResidueDetails
DSER135
DLYS161
DASN191
DILE293
ASER135
ALYS161
AASN191
AILE293
BSER135
BLYS161
BASN191
BILE293
CSER135
CLYS161
CASN191
CILE293

site_idSWS_FT_FI4
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:15134446, ECO:0000269|PubMed:23130969, ECO:0000269|Ref.9, ECO:0007744|PDB:1SJA, ECO:0007744|PDB:1SJB, ECO:0007744|PDB:1SJC, ECO:0007744|PDB:4A6G, ECO:0007744|PDB:5FJO, ECO:0007744|PDB:5FJP, ECO:0007744|PDB:5FJR, ECO:0007744|PDB:5FJT, ECO:0007744|PDB:5FJU
ChainResidueDetails
CASP239
DASP189
DGLU214
DASP239
AASP189
AGLU214
AASP239
BASP189
BGLU214
BASP239
CASP189
CGLU214

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PDB entries from 2024-06-12

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