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4XUG

Crystal structure of Tryptophan Synthase from Salmonella typhimurium in complex with 2-({[4-(Trifluoromethoxy)Phenyl]Sulfonyl}Amino)Ethyl Dihydrogen Phosphate (F9F) inhibitor in the alpha site and ammonium ion in the metal coordination site.

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 Residues20
Detailsbinding site for residue F9F A 300
ChainResidue
APHE22
ATHR183
AGLY184
APHE212
AGLY213
AILE232
AGLY234
ASER235
AHOH456
AHOH474
AHOH512
AGLU49
BPRO18
AALA59
AILE64
ALEU100
ALEU127
AALA129
AILE153
ATYR175

site_idAC2
Number of Residues19
Detailsbinding site for residue PLP B 400
ChainResidue
BHIS86
BLYS87
BGLN114
BTHR190
BCYS230
BGLY232
BGLY233
BGLY234
BSER235
BASN236
BGLY303
BGLU350
BSER377
BGLY378
BEDO402
BHOH617
BHOH705
BHOH748
BHOH838

site_idAC3
Number of Residues5
Detailsbinding site for residue NH4 B 401
ChainResidue
BGLY268
BSER297
BLEU304
BPHE306
BHOH697

site_idAC4
Number of Residues11
Detailsbinding site for residue EDO B 402
ChainResidue
BLYS87
BTHR110
BGLY111
BALA112
BGLY113
BGLN114
BHIS115
BPLP400
BHOH748
BHOH750
BHOH973

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_idMCSA1
Number of Residues3
DetailsM-CSA 383
ChainResidueDetails
BLYS87electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor
BGLU109
BSER377hydrogen bond donor

221716

PDB entries from 2024-06-26

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