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4X5E

Anthranilate phosphoribosyltransferase variant R194A from Mycobacterium tuberculosis with pyrophosphate, Mg2+ and anthranilate bound

Functional Information from GO Data
ChainGOidnamespacecontents
A0000162biological_processL-tryptophan biosynthetic process
A0000287molecular_functionmagnesium ion binding
A0004048molecular_functionanthranilate phosphoribosyltransferase activity
A0005576cellular_componentextracellular region
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0008652biological_processamino acid biosynthetic process
A0009073biological_processaromatic amino acid family biosynthetic process
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0046872molecular_functionmetal ion binding
B0000162biological_processL-tryptophan biosynthetic process
B0000287molecular_functionmagnesium ion binding
B0004048molecular_functionanthranilate phosphoribosyltransferase activity
B0005576cellular_componentextracellular region
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0008652biological_processamino acid biosynthetic process
B0009073biological_processaromatic amino acid family biosynthetic process
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0016763molecular_functionpentosyltransferase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues17
Detailsbinding site for residue POP A 401
ChainResidue
AVAL106
AMG402
AMG403
AHOH594
AHOH652
AHOH653
AHOH713
AHOH714
AHOH727
AGLY107
AASN117
ALEU118
ASER119
ATHR120
ALYS135
AGLY147
AGLU252

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 402
ChainResidue
ASER119
AGLU252
APOP401
AMG403
AHOH586
AHOH594

site_idAC3
Number of Residues8
Detailsbinding site for residue MG A 403
ChainResidue
AASP251
AGLU252
APOP401
AMG402
AHOH594
AHOH598
AHOH612
AHOH652

site_idAC4
Number of Residues10
Detailsbinding site for residue BE2 A 404
ChainResidue
AVAL106
AGLY107
ATHR108
AHIS136
AASN138
AARG193
AGLY206
ABE2405
AHOH638
AHOH755

site_idAC5
Number of Residues11
Detailsbinding site for residue BE2 A 405
ChainResidue
AMET86
AASN138
AALA179
APRO180
ATYR186
AARG193
AGLY206
ABE2404
AHOH626
AHOH639
AHOH670

site_idAC6
Number of Residues12
Detailsbinding site for residue GOL A 406
ChainResidue
AARG215
AALA236
AARG237
AARG238
ALEU305
AGLY306
AGLY307
AILE351
AASP352
AGLU357
AHOH522
AHOH817

site_idAC7
Number of Residues6
Detailsbinding site for residue GOL A 407
ChainResidue
AGLY43
AALA46
ATRP47
AASP50
AARG346
AHOH530

site_idAC8
Number of Residues11
Detailsbinding site for residue POP B 401
ChainResidue
BVAL106
BGLY107
BASN117
BSER119
BTHR120
BLYS135
BGLU252
BMG402
BMG403
BHOH593
BHOH682

site_idAC9
Number of Residues6
Detailsbinding site for residue MG B 402
ChainResidue
BSER119
BGLU252
BPOP401
BMG403
BHOH586
BHOH682

site_idAD1
Number of Residues7
Detailsbinding site for residue MG B 403
ChainResidue
BTHR115
BASP251
BGLU252
BPOP401
BMG402
BHOH622
BHOH682

site_idAD2
Number of Residues6
Detailsbinding site for residue BE2 B 404
ChainResidue
BALA190
BASN138
BPRO180
BHIS183
BTYR186
BARG187

site_idAD3
Number of Residues7
Detailsbinding site for residue BE2 B 405
ChainResidue
BGLY137
BASN138
BGLY206
BHOH637
BHOH649
BHOH660
BHOH673

site_idAD4
Number of Residues6
Detailsbinding site for residue GOL B 406
ChainResidue
BGLY43
BALA46
BTRP47
BASP50
BGLU342
BARG346

site_idAD5
Number of Residues8
Detailsbinding site for residue GOL B 407
ChainResidue
BARG237
BARG238
BLEU305
BGLY306
BGLY307
BILE351
BASP352
BGLU357

site_idAD6
Number of Residues2
Detailsbinding site for residue GOL B 408
ChainResidue
BARG263
BVAL325

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00211
ChainResidueDetails
AGLY107
BGLY107

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING:
ChainResidueDetails
AGLY110
BASN117
BSER119
BLYS135
BASN138
BARG193
BASP251
BGLU252
AASN117
ASER119
ALYS135
AASN138
AARG193
AASP251
AGLU252
BGLY110

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00211, ECO:0000269|PubMed:16337227, ECO:0000269|PubMed:23363292, ECO:0000269|Ref.4, ECO:0000269|Ref.5
ChainResidueDetails
ATHR115
AGLY147
BTHR115
BGLY147

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:21969609
ChainResidueDetails
AALA2
BALA2

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PDB entries from 2025-06-18

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