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2TSY

CRYSTAL STRUCTURES OF MUTANT (BETAK87T) TRYPTOPHAN SYNTHASE ALPHA2 BETA2 COMPLEX WITH LIGANDS BOUND TO THE ACTIVE SITES OF THE ALPHA AND BETA SUBUNITS REVEAL LIGAND-INDUCED CONFORMATIONAL CHANGES

Functional Information from GO Data
ChainGOidnamespacecontents
A0000162biological_processtryptophan biosynthetic process
A0004834molecular_functiontryptophan synthase activity
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0006568biological_processtryptophan metabolic process
A0016829molecular_functionlyase activity
B0000162biological_processtryptophan biosynthetic process
B0004834molecular_functiontryptophan synthase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0006568biological_processtryptophan metabolic process
B0016829molecular_functionlyase activity
B0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 400
ChainResidue
BGLY232
BPHE306
BSER308
BHOH425
BHOH442

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE G3P A 271
ChainResidue
ATHR183
AGLY184
APHE212
AGLY213
AGLY234
ASER235
APHE22
ATYR175

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PLS B 398
ChainResidue
BTHR110
BGLY111
BALA112
BGLY113
BGLN114
BHIS115
BTHR190
BGLY232
BGLY233
BGLY234
BSER235
BASN236
BGLY303
BLEU304
BGLU350
BSER377

site_idS1
Number of Residues1
DetailsPRODUCT ANALOG BOUND TO THE ALPHA ACTIVE SITE.
ChainResidue
AG3P271

site_idS2
Number of Residues1
DetailsREACTION INTERMEDIATE BOUND TO THE BETA ACTIVE SITE.
ChainResidue
BPLS398

Functional Information from PROSITE/UniProt
site_idPS00167
Number of Residues14
DetailsTRP_SYNTHASE_ALPHA Tryptophan synthase alpha chain signature. LELGvPFSDPLADG
ChainResidueDetails
ALEU48-GLY61

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
BTHR88
AASP60

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a50
ChainResidueDetails
BHIS86
BTHR87
BLYS167
BASP305

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a50
ChainResidueDetails
BTHR87

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a50
ChainResidueDetails
ATYR175
AGLU49
AASP60

site_idMCSA1
Number of Residues3
DetailsM-CSA 383
ChainResidueDetails
BTHR88electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor
BTHR110
BGLY378hydrogen bond donor

226707

PDB entries from 2024-10-30

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