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1I7Q

ANTHRANILATE SYNTHASE FROM S. MARCESCENS

Functional Information from GO Data
ChainGOidnamespacecontents
A0000162biological_processL-tryptophan biosynthetic process
A0004049molecular_functionanthranilate synthase activity
A0005515molecular_functionprotein binding
A0008652biological_processamino acid biosynthetic process
A0009058biological_processbiosynthetic process
A0009073biological_processaromatic amino acid family biosynthetic process
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
B0000162biological_processL-tryptophan biosynthetic process
B0002047biological_processphenazine biosynthetic process
B0003824molecular_functioncatalytic activity
B0004048molecular_functionanthranilate phosphoribosyltransferase activity
B0004049molecular_functionanthranilate synthase activity
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0008652biological_processamino acid biosynthetic process
B0009073biological_processaromatic amino acid family biosynthetic process
B0016829molecular_functionlyase activity
C0000162biological_processL-tryptophan biosynthetic process
C0004049molecular_functionanthranilate synthase activity
C0005515molecular_functionprotein binding
C0008652biological_processamino acid biosynthetic process
C0009058biological_processbiosynthetic process
C0009073biological_processaromatic amino acid family biosynthetic process
C0016829molecular_functionlyase activity
C0046872molecular_functionmetal ion binding
D0000162biological_processL-tryptophan biosynthetic process
D0002047biological_processphenazine biosynthetic process
D0003824molecular_functioncatalytic activity
D0004048molecular_functionanthranilate phosphoribosyltransferase activity
D0004049molecular_functionanthranilate synthase activity
D0005515molecular_functionprotein binding
D0005829cellular_componentcytosol
D0008652biological_processamino acid biosynthetic process
D0009073biological_processaromatic amino acid family biosynthetic process
D0016829molecular_functionlyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1701
ChainResidue
AGLU361
AGLU498
ABEZ1501
AHOH1760
AHOH1898

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG C 1702
ChainResidue
CHOH1719
CGLU361
CGLU498
CBEZ1502
CHOH1716

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GLU B 1401
ChainResidue
AGLY259
BPRO57
BGLY58
BPRO59
BGLY60
BCYS85
BLEU86
BGLN89
BTYR133
BHIS134
BSER135
BLEU136
BHOH1547

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GLU D 1402
ChainResidue
CGLY259
DPRO57
DGLY58
DPRO59
DGLY60
DCYS85
DLEU86
DGLN89
DTYR133
DHIS134
DSER135
DLEU136

site_idAC5
Number of Residues14
DetailsBINDING SITE FOR RESIDUE BEZ A 1501
ChainResidue
AGLU309
AILE326
AGLY328
ATHR329
AGLU361
ATHR425
AARG469
AALA484
AGLY485
AGLU498
ALYS502
APYR1601
AMG1701
AHOH1881

site_idAC6
Number of Residues14
DetailsBINDING SITE FOR RESIDUE BEZ C 1502
ChainResidue
CGLU309
CILE326
CGLY328
CTHR329
CGLU361
CHIS398
CTHR425
CARG469
CGLY485
CGLU498
CLYS502
CPYR1602
CMG1702
CHOH1922

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PYR A 1601
ChainResidue
ATYR449
AILE468
AARG469
AALA482
AGLY483
ALYS502
ABEZ1501
AHOH1702

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PYR C 1602
ChainResidue
CVAL265
CTYR449
CILE468
CARG469
CALA482
CGLY483
CLYS502
CBEZ1502
CHOH1711

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11371633","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1I7S","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11371633","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11371633","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues380
DetailsDomain: {"description":"Glutamine amidotransferase type-1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00605","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsActive site: {"description":"Nucleophile; for GATase activity","evidences":[{"source":"PubMed","id":"11371633","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsActive site: {"description":"For GATase activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU00605","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 11371633
ChainResidueDetails
AHIS398
BCYS85
BHIS172
BGLU174

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PDB entries from 2026-01-14

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