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1I1Q

STRUCTURE OF THE COOPERATIVE ALLOSTERIC ANTHRANILATE SYNTHASE FROM SALMONELLA TYPHIMURIUM

Functional Information from GO Data
ChainGOidnamespacecontents
A0000162biological_processtryptophan biosynthetic process
A0004049molecular_functionanthranilate synthase activity
A0009058biological_processbiosynthetic process
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE TRP A 1001
ChainResidue
ALEU38
AASP463
AHOH1008
AHOH1030
AGLU39
ASER40
ALEU49
ALYS50
APRO291
ATYR292
AMET293
AVAL453

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile; for GATase activity => ECO:0000250|UniProtKB:P00900
ChainResidueDetails
BLEU84
ALYS50

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: For GATase activity => ECO:0000250
ChainResidueDetails
BPRO170
BSER172

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00900
ChainResidueDetails
BPRO57
BALA88
BLEU134
AARG469
AGLY483
AGLY485
AGLU498

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1bxr
ChainResidueDetails
AHIS398

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bxr
ChainResidueDetails
BCYS83
BHIS169
BGLU171

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bxr
ChainResidueDetails
BCYS83
BHIS169

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PDB entries from 2024-07-17

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