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1KFK

Crystal structure of Tryptophan Synthase From Salmonella Typhimurium

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 415
ChainResidue
BGLY232
BPHE306
BSER308
BHOH568
BHOH569

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE PLP B 400
ChainResidue
BCYS230
BGLY232
BGLY233
BGLY234
BSER235
BASN236
BGLY303
BGLU350
BSER377
BGLY378
BHOH418
BHOH558
BHOH560
BHOH561
BHIS86
BLYS87
BGLN114
BTHR190

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

site_idPS00168
Number of Residues15
DetailsTRP_SYNTHASE_BETA Tryptophan synthase beta chain pyridoxal-phosphate attachment site. LlHgGAHKtNqvLgQ
ChainResidueDetails
BLEU80-GLN94

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
BLYS87
AASP60

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a50
ChainResidueDetails
BHIS86
BLYS87
BLYS167
BASP305

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a50
ChainResidueDetails
BLYS87

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a50
ChainResidueDetails
BSER377
BLYS87

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a50
ChainResidueDetails
ATYR175
AGLU49
AASP60

site_idMCSA1
Number of Residues3
DetailsM-CSA 383
ChainResidueDetails
BLYS87electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor
BGLU109
BSER377hydrogen bond donor

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PDB entries from 2024-07-17

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