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4ZQC

Tryptophan Synthase from Salmonella typhimurium in complex with two molecules of N-(4'-trifluoromethoxybenzoyl)-2-amino-1-ethylphosphate (F6F) inhibitor in the alpha-site and a single F6F molecule in the beta-site at 1.54 Angstrom resolution.

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 Residues18
Detailsbinding site for residue F6F A 301
ChainResidue
AGLU49
AGLY213
AGLY234
ASER235
AF6F302
AHOH415
AHOH418
AHOH433
AHOH675
BPRO18
AALA59
AASP60
ALEU100
ALEU127
AALA129
AILE153
ATYR175
APHE212

site_idAC2
Number of Residues17
Detailsbinding site for residue F6F A 302
ChainResidue
ALEU58
AALA59
AASP60
AGLY61
AILE64
AARG179
APHE212
ASER235
AF6F301
AHOH433
AHOH464
BPRO18
BILE20
BLEU21
BLEU174
BARG175
BSER178

site_idAC3
Number of Residues7
Detailsbinding site for residue DMS A 303
ChainResidue
APHE22
ATHR24
AGLY51
AVAL52
AASP60
AASN68
ALEU100

site_idAC4
Number of Residues7
Detailsbinding site for residue DMS A 304
ChainResidue
AMET1
AASN147
AILE148
AALA149
AARG171
AHOH429
AHOH523

site_idAC5
Number of Residues1
Detailsbinding site for residue DMS A 305
ChainResidue
AGLU16

site_idAC6
Number of Residues19
Detailsbinding site for residue PLP B 401
ChainResidue
BALA85
BHIS86
BLYS87
BGLN114
BTHR190
BCYS230
BGLY232
BGLY233
BGLY234
BSER235
BASN236
BGLY303
BGLU350
BSER377
BGLY378
BHOH521
BHOH678
BHOH683
BHOH735

site_idAC7
Number of Residues19
Detailsbinding site for residue F6F B 402
ChainResidue
BLYS87
BGLU109
BTHR110
BGLY111
BGLN114
BHIS115
BCYS170
BLEU174
BTYR186
BLEU188
BTHR190
BGLY193
BPRO194
BPHE280
BPHE306
BHOH515
BHOH521
BHOH571
BHOH709

site_idAC8
Number of Residues5
Detailsbinding site for residue NA B 403
ChainResidue
BGLY232
BPHE306
BSER308
BHOH593
BHOH697

site_idAC9
Number of Residues6
Detailsbinding site for residue DMS B 404
ChainResidue
BTHR66
BTHR69
BARG70
BTHR71
BHOH617
BHOH721

site_idAD1
Number of Residues5
Detailsbinding site for residue DMS B 405
ChainResidue
BHIS273
BMET286
BMET287
BGLN288
BHOH594

site_idAD2
Number of Residues4
Detailsbinding site for residue DMS B 406
ChainResidue
BASN51
BTHR60
BLYS61
BHOH634

site_idAD3
Number of Residues6
Detailsbinding site for residue DMS B 407
ChainResidue
BGLN42
BALA46
BMET207
BHOH942
BHOH945
BHOH974

site_idAD4
Number of Residues3
Detailsbinding site for residue DMS B 408
ChainResidue
BGLU331
BHOH527
BHOH832

site_idAD5
Number of Residues6
Detailsbinding site for residue DMS B 409
ChainResidue
BALA112
BGLN114
BGLN142
BLYS382
BASP383
BHOH614

site_idAD6
Number of Residues4
Detailsbinding site for residue DMS B 410
ChainResidue
BARG150
BARG341
BILE397
BHOH744

site_idAD7
Number of Residues4
Detailsbinding site for residue DMS B 412
ChainResidue
BGLN36
BLYS37
BASP38
BPRO39

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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