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6WX3

High resolution Tryptophan Synthase crystal structure from Salmonella typhimurium in complex with F9 inhibitor in the alpha-site, Cesium ion at the metal coordination site and internal aldimine form.

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 Residues21
Detailsbinding site for residue F9F A 301
ChainResidue
APHE22
ATHR183
AGLY184
APHE212
AGLY213
AILE232
AGLY234
ASER235
AHOH424
AHOH439
AHOH525
AGLU49
AHOH676
BPRO18
AALA59
AILE64
ALEU100
ALEU127
AALA129
AILE153
ATYR175

site_idAC2
Number of Residues5
Detailsbinding site for residue CL A 302
ChainResidue
AALA167
AGLY170
AHIS204
AHOH491
AHOH612

site_idAC3
Number of Residues17
Detailsbinding site for residue PLP B 1401
ChainResidue
BHIS86
BLYS87
BGLN114
BTHR190
BCYS230
BGLY232
BGLY233
BGLY234
BSER235
BASN236
BGLY303
BGLU350
BSER377
BGLY378
BHOH1594
BHOH1600
BHOH1646

site_idAC4
Number of Residues8
Detailsbinding site for residue CS B 1402
ChainResidue
BVAL231
BGLY232
BGLU256
BGLY268
BPRO270
BLEU304
BPHE306
BSER308

site_idAC5
Number of Residues10
Detailsbinding site for residue BCN B 1403
ChainResidue
BGLY259
BHIS260
BGLU263
BTHR328
BASP329
BASP330
BHOH1514
BHOH1534
BHOH1643
BHOH1975

site_idAC6
Number of Residues10
Detailsbinding site for residue BCN B 1404
ChainResidue
BTHR248
BVAL250
BGLY251
BLEU252
BGLY320
BARG321
BASP323
BHOH1561
BHOH1563
BHOH1665

site_idAC7
Number of Residues7
Detailsbinding site for residue BCN B 1405
ChainResidue
BTHR289
BALA290
BASP291
BGLN293
BHOH1568
BHOH1725
BHOH1769

site_idAC8
Number of Residues11
Detailsbinding site for residue BCN B 1406
ChainResidue
BLEU271
BLYS272
BGLY274
BPRO285
BARG363
BGLU364
BHOH1599
BHOH1701
BHOH1732
BHOH1756
BHOH1960

site_idAC9
Number of Residues6
Detailsbinding site for residue EDO B 1407
ChainResidue
BASP225
BGLU369
BGLN370
BHOH1561
BHOH1628
BHOH1630

site_idAD1
Number of Residues1
Detailsbinding site for residue DMS B 1408
ChainResidue
BGLY10

site_idAD2
Number of Residues1
Detailsbinding site for residue EDO B 1409
ChainResidue
BTHR3

site_idAD3
Number of Residues5
Detailsbinding site for residue CS B 1410
ChainResidue
BTHR71
BHOH1849
BHOH1873
BTHR66
BTHR69

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
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AASP60
AGLU49

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 383
ChainResidueDetails
AGLU49hydrogen bond acceptor, proton acceptor, proton donor
AASP60hydrogen bond acceptor
ATYR175hydrogen bond donor

219869

PDB entries from 2024-05-15

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