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5FJP

N-acyl amino acid racemase from Amycolatopsis sp Ts-1-60: G291D F323Y I293G mutant in complex with N-acetyl naphthylalanine

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 NPQ B 1369
ChainResidue
BPHE19
BLYS263
BASP291
BASP316
BTYR323
BMG1370
BHOH2051
BGLN26
BMET50
BSER135
BLYS161
BLYS163
BASP189
BASN191
BASP239

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE NPQ D 1368
ChainResidue
DPHE19
DGLN26
DMET50
DSER135
DLYS161
DLYS163
DASP189
DASN191
DGLU214
DASP239
DLYS263
DASP291
DASP316
DTYR323
DMG1369
DHOH2028

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE NPQ C 1368
ChainResidue
CPHE19
CGLN26
CSER135
CLYS161
CLYS163
CASP189
CASN191
CASP239
CLYS263
CASP291
CMET292
CTYR323
CMG1369

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE NPQ A 1369
ChainResidue
APHE19
AGLN26
ASER135
ALYS161
ALYS163
AASP189
AASN191
ALYS263
AASP291
AASP316
ATYR323
AMG1370
AHOH2055

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 1370
ChainResidue
ALYS161
AASP189
AASN191
AGLU214
AASP239
ANPQ1369
AHOH2062

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 1370
ChainResidue
BASP189
BGLU214
BASP239
BNPQ1369
BHOH2056

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG C 1369
ChainResidue
CASP189
CASN191
CGLU214
CASP239
CNPQ1368
CHOH2037

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG D 1369
ChainResidue
DLYS161
DASP189
DGLU214
DASP239
DNPQ1368
DHOH2031

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
ASER135
CLYS161
CASN191
CGLY293
DSER135
DLYS161
DASN191
DGLY293
ALYS161
AASN191
AGLY293
BSER135
BLYS161
BASN191
BGLY293
CSER135

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
AASP189
DASP189
DGLU214
DASP239
AGLU214
AASP239
BASP189
BGLU214
BASP239
CASP189
CGLU214
CASP239

222036

PDB entries from 2024-07-03

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