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4ZDK

Crystal structure of the M. tuberculosis CTP synthase PyrG in complex with UTP, AMP-PCP and oxonorleucine

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003883molecular_functionCTP synthase activity
A0004359molecular_functionglutaminase activity
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006221biological_processpyrimidine nucleotide biosynthetic process
A0006241biological_processCTP biosynthetic process
A0016874molecular_functionligase activity
A0019856biological_processpyrimidine nucleobase biosynthetic process
A0042802molecular_functionidentical protein binding
A0044210biological_process'de novo' CTP biosynthetic process
A0046872molecular_functionmetal ion binding
A0097268cellular_componentcytoophidium
B0000166molecular_functionnucleotide binding
B0003883molecular_functionCTP synthase activity
B0004359molecular_functionglutaminase activity
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006221biological_processpyrimidine nucleotide biosynthetic process
B0006241biological_processCTP biosynthetic process
B0016874molecular_functionligase activity
B0019856biological_processpyrimidine nucleobase biosynthetic process
B0042802molecular_functionidentical protein binding
B0044210biological_process'de novo' CTP biosynthetic process
B0046872molecular_functionmetal ion binding
B0097268cellular_componentcytoophidium
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue ONL A 601
ChainResidue
AGLY365
ATYR478
AGLY366
APHE367
ACYS393
AGLN397
AGLU416
AARG475
AHIS476
AARG477

site_idAC2
Number of Residues16
Detailsbinding site for residue ACP A 602
ChainResidue
ASER21
ALEU22
AGLY23
ALYS24
AGLY25
ALEU26
ALYS46
AASP78
AGLU152
AARG223
AASP252
AALA253
AILE256
AILE259
AMG604
BPRO194

site_idAC3
Number of Residues11
Detailsbinding site for residue UTP A 603
ChainResidue
ASER20
AGLN120
AILE122
AASP159
AILE160
AGLU161
BLEU198
BLYS199
BTHR200
BLYS201
BGLN204

site_idAC4
Number of Residues4
Detailsbinding site for residue MG A 604
ChainResidue
AGLY25
AASP78
AGLU152
AACP602

site_idAC5
Number of Residues14
Detailsbinding site for residue ACP B 602
ChainResidue
APRO194
BSER21
BLEU22
BGLY23
BLYS24
BGLY25
BLEU26
BLYS46
BASP78
BGLU152
BARG223
BALA253
BILE259
BMG604

site_idAC6
Number of Residues10
Detailsbinding site for residue UTP B 603
ChainResidue
ALYS199
ATHR200
ALYS201
AGLN204
BSER20
BGLN120
BILE122
BASP159
BILE160
BGLU161

site_idAC7
Number of Residues4
Detailsbinding site for residue MG B 604
ChainResidue
BGLY25
BASP78
BGLU152
BACP602

site_idAC8
Number of Residues16
Detailsbinding site for Di-peptide ONL B 601 and CYS B 393
ChainResidue
BGLY365
BGLY366
BLEU392
BLEU394
BGLY395
BLEU396
BGLN397
BGLU416
BARG475
BHIS476
BARG477
BTYR478
BTHR521
BGLN522
BALA523
BHIS524

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Nucleophile; for glutamine hydrolysis","evidences":[{"source":"HAMAP-Rule","id":"MF_01227","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26097035","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01227","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26097035","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26097035","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues28
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01227","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P0A7E5","evidenceCode":"ECO:0000250"},{"source":"PubMed","id":"26097035","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

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PDB entries from 2025-07-23

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