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7LEV

The aminoacrylate form of the wild-type Salmonella typhimurium Tryptophan Synthase in complex with ammonium ion at the metal coordination site at 1.70 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 Residues4
Detailsbinding site for residue DMS A 301
ChainResidue
AALA59
ALEU100
AILE153
ATYR175

site_idAC2
Number of Residues7
Detailsbinding site for residue EDO A 302
ChainResidue
AASN147
AHOH445
AMET1
AARG3
AGLU119
AGLY122
AVAL123

site_idAC3
Number of Residues4
Detailsbinding site for residue EDO A 303
ChainResidue
APHE82
AALA113
AHOH412
AHOH454

site_idAC4
Number of Residues4
Detailsbinding site for residue CL A 304
ChainResidue
AHIS92
APRO93
ATHR94
AILE95

site_idAC5
Number of Residues5
Detailsbinding site for residue DMS B 401
ChainResidue
BLYS50
BGLY54
BARG55
BTHR57
BGLN215

site_idAC6
Number of Residues3
Detailsbinding site for residue DMS B 402
ChainResidue
BLEU271
BASN317
BARG363

site_idAC7
Number of Residues2
Detailsbinding site for residue DMS B 403
ChainResidue
BGLN42
BMET207

site_idAC8
Number of Residues3
Detailsbinding site for residue DMS B 404
ChainResidue
BGLU211
BGLN215
BHOH549

site_idAC9
Number of Residues1
Detailsbinding site for residue DMS B 405
ChainResidue
BHOH527

site_idAD1
Number of Residues21
Detailsbinding site for residue 0JO B 406
ChainResidue
BALA85
BHIS86
BLYS87
BTHR110
BGLY111
BALA112
BGLY113
BGLN114
BHIS115
BTHR190
BCYS230
BGLY232
BGLY233
BGLY234
BSER235
BASN236
BGLY303
BGLU350
BSER377
BHOH574
BHOH675

site_idAD2
Number of Residues4
Detailsbinding site for residue DMS B 407
ChainResidue
BASP47
BASN51
BTHR60
BLYS61

site_idAD3
Number of Residues4
Detailsbinding site for residue DMS B 408
ChainResidue
BTHR66
BTHR69
BTHR71
BHOH745

site_idAD4
Number of Residues5
Detailsbinding site for residue EDO B 409
ChainResidue
BPHE9
BTYR315
BHOH503
BHOH581
BHOH692

site_idAD5
Number of Residues6
Detailsbinding site for residue NH4 B 410
ChainResidue
BGLY232
BGLY268
BLEU304
BPHE306
BSER308
BHOH526

site_idAD6
Number of Residues2
Detailsbinding site for residue CL B 411
ChainResidue
BGLN36
BLYS37

site_idAD7
Number of Residues2
Detailsbinding site for residue CL B 413
ChainResidue
BLEU5
BASN6

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
AGLU49
AASP60

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

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PDB entries from 2024-07-17

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