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4HT3

The crystal structure of Salmonella typhimurium Tryptophan Synthase at 1.30A complexed with N-(4'-TRIFLUOROMETHOXYBENZENESULFONYL)-2-AMINO-1-ETHYLPHOSPHATE (F9) inhibitor in the alpha site, internal aldimine

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 301
ChainResidue
APHE22
ATHR183
AGLY184
APHE212
AGLY213
AILE232
AGLY234
ASER235
AHOH406
AHOH411
AHOH415
AGLU49
BPRO18
AALA59
AILE64
ALEU100
ALEU127
AALA129
AILE153
ATYR175

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BCN A 302
ChainResidue
ASER247
APRO248
ALYS249
AGLN250

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CS A 304
ChainResidue
ASER221
AALA265
AARG267
BLYS99

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PGE A 305
ChainResidue
APHE107
AILE111
AGLU135
APRO138
APHE139
AHOH416
AHOH435
AHOH601
AHOH674
BTYR16
BLYS283

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PG5 A 306
ChainResidue
AARG164
AVAL166
AALA167
ASER168
AGLY170
AARG171
ATHR174
ATYR203
AHIS204
AALA205
AALA206
AHOH663

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 307
ChainResidue
APRO93
AALA137
AARG140
AGLN141
AEDO308
AHOH455

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 308
ChainResidue
APRO93
ATHR94
AEDO307
AHOH430

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 309
ChainResidue
AALA86
ALEU87
AGLU90
AARG171
AHOH482
AHOH487

site_idAC9
Number of Residues17
DetailsBINDING SITE FOR RESIDUE PLP B 401
ChainResidue
BHIS86
BLYS87
BGLN114
BTHR190
BCYS230
BGLY232
BGLY233
BGLY234
BSER235
BASN236
BGLY303
BGLU350
BSER377
BGLY378
BHOH502
BHOH684
BHOH937

site_idBC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO B 402
ChainResidue
BLYS87
BTHR110
BGLY111
BALA112
BGLY113
BGLN114
BHIS115
BEDO419

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PGE B 403
ChainResidue
BHOH893
BLEU271
BLYS272
BGLY274
BPRO285
BASN317
BGLU364
BCL423

site_idBC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 404
ChainResidue
BALA67

site_idBC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE BCN B 405
ChainResidue
BGLY259
BHIS260
BGLU263
BTHR328
BASP329
BASP330
BEDO413
BEDO414
BHOH539
BHOH771
BHOH773
BHOH897
BHOH904

site_idBC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE BCN B 406
ChainResidue
BTHR248
BVAL250
BGLY251
BLEU252
BGLY320
BARG321
BASP323
BHOH780
BHOH803
BHOH856

site_idBC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE BCN B 407
ChainResidue
BTHR289
BALA290
BASP291
BGLN293
BHOH581
BHOH599
BHOH764

site_idBC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 408
ChainResidue
BVAL117

site_idBC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 409
ChainResidue
BASP47
BLYS61
BLYS219
BPEG416
BHOH522
BHOH553
BHOH795

site_idBC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 410
ChainResidue
BHIS273
BVAL325
BSER326
BHOH578
BHOH664
BHOH716
BHOH794

site_idCC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CS B 411
ChainResidue
BTHR66
BTHR69
BTHR71
BHOH822
BHOH948

site_idCC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CS B 412
ChainResidue
BVAL231
BGLY232
BGLU256
BGLY268
BPRO270
BLEU304
BPHE306
BSER308

site_idCC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 413
ChainResidue
BASP330
BGLU331
BBCN405
BEDO414
BHOH586
BHOH693
BHOH771

site_idCC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 414
ChainResidue
BTHR328
BBCN405
BEDO413

site_idCC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG B 415
ChainResidue
BTHR3
BLEU4
BASN6

site_idCC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PEG B 416
ChainResidue
BASN51
BTYR52
BTHR60
BLYS61
BLEU125
BGLU343
BEDO409
BHOH870

site_idCC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PGE B 417
ChainResidue
BGLU211
BALA214
BGLN215
BHOH524
BHOH544
BHOH605
BHOH751
BHOH756

site_idCC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 418
ChainResidue
BGLY10

site_idCC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 419
ChainResidue
BGLU109
BGLY189
BPHE306
BEDO402

site_idDC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 420
ChainResidue
BASP225
BHOH528

site_idDC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 421
ChainResidue
BHOH669
BHOH759
BHOH852

site_idDC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 422
ChainResidue
BASP225
BSER249
BHOH821

site_idDC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 423
ChainResidue
BPHE12
BPRO285
BPGE403
BHOH516
BHOH739

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

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PDB entries from 2024-11-06

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