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6WDU

The external aldimine form of the Salmonella thypi wild-type tryptophan synthase in open conformation showing multiple side chain conformations for the residue beta Q114 and sodium ion at the metal coordination site. One of the beta-Q114 rotamer conformations allows a hydrogen bond to form with the PLP oxygen at the position 3 in the ring.

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 Residues4
Detailsbinding site for residue EDO A 301
ChainResidue
AARG225
AARG267
BLYS99
BHOH731

site_idAC2
Number of Residues2
Detailsbinding site for residue EDO A 302
ChainResidue
APHE258
BGLU182

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO A 303
ChainResidue
ATHR94
AILE95
AILE41
AHIS92
APRO93

site_idAC4
Number of Residues3
Detailsbinding site for residue DMS A 304
ChainResidue
APHE82
AHOH479
AHOH508

site_idAC5
Number of Residues5
Detailsbinding site for residue DMS A 305
ChainResidue
AASP60
AALA129
AILE153
AHOH428
AHOH655

site_idAC6
Number of Residues5
Detailsbinding site for residue DMS A 306
ChainResidue
AGLU5
AASN147
AILE148
AALA149
AHOH484

site_idAC7
Number of Residues7
Detailsbinding site for residue PEG B 401
ChainResidue
BGLY10
BGLU11
BPHE12
BLYS283
BHOH558
BHOH694
BHOH789

site_idAC8
Number of Residues5
Detailsbinding site for residue EDO B 402
ChainResidue
BPRO56
BGLU211
BHOH526
BHOH723
BHOH768

site_idAC9
Number of Residues6
Detailsbinding site for residue EDO B 403
ChainResidue
BPHE9
BTYR315
BHOH529
BHOH582
BHOH717
BHOH803

site_idAD1
Number of Residues10
Detailsbinding site for residue PEG B 404
ChainResidue
BASN51
BLEU59
BTHR60
BLYS61
BGLN63
BLEU125
BLYS219
BHOH508
BHOH609
BHOH857

site_idAD2
Number of Residues3
Detailsbinding site for residue EDO B 405
ChainResidue
BGLN36
BGLN42
BDMS414

site_idAD3
Number of Residues3
Detailsbinding site for residue EDO B 406
ChainResidue
BLYS219
BGLU220
BGLY221

site_idAD4
Number of Residues5
Detailsbinding site for residue NA B 407
ChainResidue
BGLY232
BPHE306
BSER308
BHOH628
BHOH704

site_idAD5
Number of Residues5
Detailsbinding site for residue NA B 408
ChainResidue
BTHR66
BTHR69
BTHR71
BHOH756
BHOH832

site_idAD6
Number of Residues5
Detailsbinding site for residue EDO B 409
ChainResidue
BGLU210
BDMS413
BHOH573
BHOH576
BHOH578

site_idAD7
Number of Residues22
Detailsbinding site for residue KOU B 410
ChainResidue
BHIS86
BLYS87
BTHR110
BGLY111
BALA112
BGLY113
BGLN114
BHIS115
BTHR190
BGLY232
BGLY233
BGLY234
BSER235
BASN236
BGLY303
BASP305
BGLU350
BSER377
BHOH501
BHOH650
BHOH651
BHOH799

site_idAD8
Number of Residues4
Detailsbinding site for residue DMS B 411
ChainResidue
BGLN42
BALA46
BHOH723
BHOH901

site_idAD9
Number of Residues7
Detailsbinding site for residue DMS B 412
ChainResidue
BLEU271
BASN317
BARG363
BGLU364
BDMS420
BHOH516
BHOH564

site_idAE1
Number of Residues1
Detailsbinding site for residue DMS B 413
ChainResidue
BEDO409

site_idAE2
Number of Residues4
Detailsbinding site for residue DMS B 414
ChainResidue
BGLN36
BLYS37
BPRO39
BEDO405

site_idAE3
Number of Residues3
Detailsbinding site for residue DMS B 415
ChainResidue
BTHR3
BLEU4
BLEU5

site_idAE4
Number of Residues2
Detailsbinding site for residue DMS B 416
ChainResidue
BHOH861
BHOH866

site_idAE5
Number of Residues5
Detailsbinding site for residue DMS B 417
ChainResidue
BTYR8
BGLY10
BGLU11
BHOH581
BHOH788

site_idAE6
Number of Residues3
Detailsbinding site for residue DMS B 418
ChainResidue
BILE262
BHIS267
BHOH843

site_idAE7
Number of Residues3
Detailsbinding site for residue DMS B 419
ChainResidue
BSER143
BPHE385
BHIS388

site_idAE8
Number of Residues7
Detailsbinding site for residue DMS B 420
ChainResidue
BLEU271
BLYS272
BGLY274
BARG275
BVAL276
BPRO285
BDMS412

site_idAE9
Number of Residues8
Detailsbinding site for residue DMS B 421
ChainResidue
APHE107
APRO138
APHE139
BTYR16
BLYS283
BHOH581
BHOH788
BHOH955

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

222926

PDB entries from 2024-07-24

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