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1WXJ

Crystal Structure Of Tryptophan Synthase A-Subunit with Indole-3-propanol phosphate From Thermus Thermophilus Hb8

Functional Information from GO Data
ChainGOidnamespacecontents
A0000162biological_processL-tryptophan biosynthetic process
A0004834molecular_functiontryptophan synthase activity
A0005829cellular_componentcytosol
A0006568biological_processL-tryptophan metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 2001
ChainResidue
ATHR90
AGLU91
ALYS92
AHOH2028
AHOH2188
AHOH2189
AHOH2212

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 2002
ChainResidue
AARG234
AARG64
AARG200

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 2003
ChainResidue
ASER212
AGLY213
AALA215
ATHR216
AHOH2065
AHOH2131
AHOH2132

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 2004
ChainResidue
ASER75
AVAL76
ATRP106
AHOH2033
AHOH2253
AHOH2258

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE IPL A 1001
ChainResidue
ATYR21
AMET97
ATYR99
ATYR172
AGLY208
APHE209
AGLY210
AGLY229
ASER230
AHOH2014

Functional Information from PROSITE/UniProt
site_idPS00167
Number of Residues14
DetailsTRP_SYNTHASE_ALPHA Tryptophan synthase alpha chain signature. LEIGlPYSDPLGDG
ChainResidueDetails
ALEU46-GLY59

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00131","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1geq
ChainResidueDetails
ATYR172
AGLU47

251422

PDB entries from 2026-04-01

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