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4HPJ

Crystal structure of Tryptophan Synthase at 1.45 A resolution in complex with 2-aminophenol quinonoid in the beta site and the F9 inhibitor in the alpha site

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
AHOH411
AHOH418
AHOH490
AGLU49
BPRO18
AALA59
AILE64
ALEU100
ALEU127
AALA129
AILE153
ATYR175

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 302
ChainResidue
AHOH430
BHOH651

site_idAC3
Number of Residues23
DetailsBINDING SITE FOR RESIDUE 1D0 B 401
ChainResidue
BHIS86
BLYS87
BGLU109
BTHR110
BGLY111
BALA112
BGLY113
BGLN114
BHIS115
BLEU166
BGLY189
BTHR190
BCYS230
BGLY232
BGLY233
BGLY234
BSER235
BASN236
BGLY303
BGLU350
BSER377
BGLY378
BHOH525

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE BCN B 402
ChainResidue
BTHR248
BVAL250
BGLY251
BLEU252
BGLY320
BARG321
BASP323
BHOH755
BHOH767
BHOH824

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG B 403
ChainResidue
BTHR3
BLEU4
BLEU5
BASN6

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PEG B 404
ChainResidue
BTHR328
BASP330
BGLU331
BHOH550
BHOH777
BHOH786

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PEG B 405
ChainResidue
BPRO56
BHOH704

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PEG B 406
ChainResidue
BLEU217
BASP218
BLYS219
BGLU220
BGLY221
BHOH882

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 407
ChainResidue
BASN6
BHOH859

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 408
ChainResidue
BPHE9
BHOH578
BHOH892

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 411
ChainResidue
AHOH466
BILE20
BTYR181

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 412
ChainResidue
BHOH566
BHOH810
BHOH895

site_idBC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CS B 413
ChainResidue
BVAL231
BGLY232
BGLU256
BGLY268
BLEU304
BPHE306
BSER308

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CS B 414
ChainResidue
BTHR66
BTHR69
BTHR71
BHOH875
BHOH876

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

225158

PDB entries from 2024-09-18

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