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1GEQ

Entropic stabilization of the tryptophan synthase A-subunit from a hyperthermophile, pyrococcus furiosus: X-ray analysis and calorimetry

Functional Information from GO Data
ChainGOidnamespacecontents
A0000162biological_processL-tryptophan biosynthetic process
A0004834molecular_functiontryptophan synthase activity
A0005829cellular_componentcytosol
A0006568biological_processL-tryptophan metabolic process
A0008652biological_processamino acid biosynthetic process
A0009073biological_processaromatic amino acid family biosynthetic process
A0016829molecular_functionlyase activity
B0000162biological_processL-tryptophan biosynthetic process
B0004834molecular_functiontryptophan synthase activity
B0005829cellular_componentcytosol
B0006568biological_processL-tryptophan metabolic process
B0008652biological_processamino acid biosynthetic process
B0009073biological_processaromatic amino acid family biosynthetic process
B0016829molecular_functionlyase activity
Functional Information from PROSITE/UniProt
site_idPS00167
Number of Residues14
DetailsTRP_SYNTHASE_ALPHA Tryptophan synthase alpha chain signature. IELGiPFSDPIADG
ChainResidueDetails
AILE35-GLY48

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 10504236
ChainResidueDetails
AASP47
ATYR161
AGLU36

site_idCSA2
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 10504236
ChainResidueDetails
BASP47
BTYR161
BGLU36

238895

PDB entries from 2025-07-16

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