Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6VNT

Tryptophan synthase in complex with inhibitor N-(4'-trifluoromethoxybenzenesulfonyl)-2-amino-1-ethylphosphate (F9F) at the alpha-site, aminoacrylate at the beta site, and sodium ion at the metal coordination site at 1.25 Angstrom resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000162biological_processL-tryptophan biosynthetic process
A0003824molecular_functioncatalytic activity
A0004834molecular_functiontryptophan synthase activity
A0005515molecular_functionprotein binding
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
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0006568biological_processL-tryptophan metabolic process
B0008652biological_processamino acid biosynthetic process
B0009073biological_processaromatic amino acid family biosynthetic process
B0016829molecular_functionlyase activity
B0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues1
Detailsbinding site for residue EDO A 301
ChainResidue
AVAL224

site_idAC2
Number of Residues19
Detailsbinding site for residue F9F A 302
ChainResidue
ATYR175
ATHR183
AGLY184
APHE212
AGLY213
AGLY234
ASER235
AHOH417
AHOH444
AHOH549
APHE22
BPRO18
AGLU49
AALA59
AILE64
ALEU100
ALEU127
AALA129
AILE153

site_idAC3
Number of Residues22
Detailsbinding site for residue 0JO B 501
ChainResidue
BHIS86
BLYS87
BTHR110
BGLY111
BALA112
BGLY113
BGLN114
BHIS115
BTHR190
BCYS230
BGLY232
BGLY233
BGLY234
BSER235
BASN236
BGLY303
BGLU350
BSER377
BGLY378
BHOH757
BHOH842
BHOH850

site_idAC4
Number of Residues7
Detailsbinding site for residue EDO B 502
ChainResidue
BHIS260
BTHR328
BASP330
BGLU331
BHOH678
BHOH708
BHOH861

site_idAC5
Number of Residues7
Detailsbinding site for residue EDO B 503
ChainResidue
BTYR52
BTHR60
BLYS61
BGLN63
BLEU125
BGLU343
BHOH628

site_idAC6
Number of Residues5
Detailsbinding site for residue EDO B 504
ChainResidue
BTHR66
BTHR69
BARG70
BTHR71
BHOH755

site_idAC7
Number of Residues4
Detailsbinding site for residue EDO B 505
ChainResidue
BGLY10
BHOH642
BHOH876
BHOH889

site_idAC8
Number of Residues6
Detailsbinding site for residue NA B 506
ChainResidue
BVAL231
BGLY232
BGLU256
BGLY268
BSER308
BHOH748

site_idAC9
Number of Residues4
Detailsbinding site for residue PEG B 507
ChainResidue
BGLN215
BHOH709
BHOH775
BHOH833

site_idAD1
Number of Residues2
Detailsbinding site for residue PEG B 508
ChainResidue
AALA246
BLEU4

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 Residues2
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine"}
ChainResidueDetails

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

239149

PDB entries from 2025-07-23

PDB statisticsPDBj update infoContact PDBjnumon