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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1PKX

Crystal Structure of human ATIC in complex with XMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0003360biological_processbrainstem development
A0003824molecular_functioncatalytic activity
A0003937molecular_functionIMP cyclohydrolase activity
A0004643molecular_functionphosphoribosylaminoimidazolecarboxamide formyltransferase activity
A0005829cellular_componentcytosol
A0006139biological_processnucleobase-containing compound metabolic process
A0006164biological_processpurine nucleotide biosynthetic process
A0006177biological_processGMP biosynthetic process
A0006189biological_process'de novo' IMP biosynthetic process
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0016787molecular_functionhydrolase activity
A0021549biological_processcerebellum development
A0021987biological_processcerebral cortex development
A0031100biological_processanimal organ regeneration
A0042803molecular_functionprotein homodimerization activity
A0044208biological_process'de novo' AMP biosynthetic process
A0045296molecular_functioncadherin binding
A0046452biological_processdihydrofolate metabolic process
A0046654biological_processtetrahydrofolate biosynthetic process
A0070062cellular_componentextracellular exosome
A0097294biological_process'de novo' XMP biosynthetic process
B0003360biological_processbrainstem development
B0003824molecular_functioncatalytic activity
B0003937molecular_functionIMP cyclohydrolase activity
B0004643molecular_functionphosphoribosylaminoimidazolecarboxamide formyltransferase activity
B0005829cellular_componentcytosol
B0006139biological_processnucleobase-containing compound metabolic process
B0006164biological_processpurine nucleotide biosynthetic process
B0006177biological_processGMP biosynthetic process
B0006189biological_process'de novo' IMP biosynthetic process
B0016020cellular_componentmembrane
B0016740molecular_functiontransferase activity
B0016787molecular_functionhydrolase activity
B0021549biological_processcerebellum development
B0021987biological_processcerebral cortex development
B0031100biological_processanimal organ regeneration
B0042803molecular_functionprotein homodimerization activity
B0044208biological_process'de novo' AMP biosynthetic process
B0045296molecular_functioncadherin binding
B0046452biological_processdihydrofolate metabolic process
B0046654biological_processtetrahydrofolate biosynthetic process
B0070062cellular_componentextracellular exosome
B0097294biological_process'de novo' XMP biosynthetic process
C0003360biological_processbrainstem development
C0003824molecular_functioncatalytic activity
C0003937molecular_functionIMP cyclohydrolase activity
C0004643molecular_functionphosphoribosylaminoimidazolecarboxamide formyltransferase activity
C0005829cellular_componentcytosol
C0006139biological_processnucleobase-containing compound metabolic process
C0006164biological_processpurine nucleotide biosynthetic process
C0006177biological_processGMP biosynthetic process
C0006189biological_process'de novo' IMP biosynthetic process
C0016020cellular_componentmembrane
C0016740molecular_functiontransferase activity
C0016787molecular_functionhydrolase activity
C0021549biological_processcerebellum development
C0021987biological_processcerebral cortex development
C0031100biological_processanimal organ regeneration
C0042803molecular_functionprotein homodimerization activity
C0044208biological_process'de novo' AMP biosynthetic process
C0045296molecular_functioncadherin binding
C0046452biological_processdihydrofolate metabolic process
C0046654biological_processtetrahydrofolate biosynthetic process
C0070062cellular_componentextracellular exosome
C0097294biological_process'de novo' XMP biosynthetic process
D0003360biological_processbrainstem development
D0003824molecular_functioncatalytic activity
D0003937molecular_functionIMP cyclohydrolase activity
D0004643molecular_functionphosphoribosylaminoimidazolecarboxamide formyltransferase activity
D0005829cellular_componentcytosol
D0006139biological_processnucleobase-containing compound metabolic process
D0006164biological_processpurine nucleotide biosynthetic process
D0006177biological_processGMP biosynthetic process
D0006189biological_process'de novo' IMP biosynthetic process
D0016020cellular_componentmembrane
D0016740molecular_functiontransferase activity
D0016787molecular_functionhydrolase activity
D0021549biological_processcerebellum development
D0021987biological_processcerebral cortex development
D0031100biological_processanimal organ regeneration
D0042803molecular_functionprotein homodimerization activity
D0044208biological_process'de novo' AMP biosynthetic process
D0045296molecular_functioncadherin binding
D0046452biological_processdihydrofolate metabolic process
D0046654biological_processtetrahydrofolate biosynthetic process
D0070062cellular_componentextracellular exosome
D0097294biological_process'de novo' XMP biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE K A 2001
ChainResidue
AVAL425
ATHR428
ASER430
ASER432
AASP539
ALEU589
AHIS591
site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K B 2002
ChainResidue
BSER430
BSER432
BASP539
BLEU589
BVAL425
BTHR428
site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE K C 2003
ChainResidue
CVAL425
CTHR428
CSER430
CSER432
CASP539
CLEU589
CHIS591
site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE K D 2004
ChainResidue
DVAL425
DTHR428
DSER430
DSER432
DASP539
DLEU589
DHIS591
site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE XMP A 1901
ChainResidue
ASER10
AVAL11
ASER12
ALYS14
ASER34
AGLY36
ATHR37
AARG64
ALYS66
ATHR67
ACYS101
AASN102
ALEU103
ATYR104
AASP125
AILE126
AGLY127
AGLY128
site_idAC6
Number of Residues19
DetailsBINDING SITE FOR RESIDUE XMP C 1903
ChainResidue
CSER10
CVAL11
CSER12
CLYS14
CSER34
CGLY36
CTHR37
CARG64
CLYS66
CTHR67
CCYS101
CASN102
CLEU103
CTYR104
CASP125
CILE126
CGLY127
CGLY128
CHOH2074
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton donor/acceptor; for FAICAR cyclization activity","evidences":[{"source":"PubMed","id":"14756553","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton acceptor; for AICAR formyltransferase activity","evidences":[{"source":"PubMed","id":"14966129","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues40
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"14756553","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"14966129","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1P4R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PKX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PL0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"14966129","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1P4R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PL0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues12
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"14966129","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29072452","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1P4R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PL0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"14966129","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29072452","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1P4R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PL0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P31335","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"14966129","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues786
DetailsRegion: {"description":"AICAR formyltransferase","evidences":[{"source":"UniProtKB","id":"P31335","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1p4r
ChainResidueDetails
AASN431
ALYS266
AHIS592
AHIS267
site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1p4r
ChainResidueDetails
BASN431
BLYS266
BHIS592
BHIS267
site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1p4r
ChainResidueDetails
CASN431
CLYS266
CHIS592
CHIS267
site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1p4r
ChainResidueDetails
DASN431
DLYS266
DHIS592
DHIS267
site_idMCSA1
Number of Residues4
DetailsM-CSA 646
ChainResidueDetails
ALYS266electrostatic stabiliser, proton acceptor, proton donor, proton relay
AHIS267electrostatic stabiliser, proton acceptor, proton donor, proton relay
AASN431electrostatic stabiliser, modifies pKa
AHIS592electrostatic stabiliser, modifies pKa, proton acceptor, proton donor, proton relay
site_idMCSA2
Number of Residues4
DetailsM-CSA 646
ChainResidueDetails
BLYS266electrostatic stabiliser, proton acceptor, proton donor, proton relay
BHIS267electrostatic stabiliser, proton acceptor, proton donor, proton relay
BASN431electrostatic stabiliser, modifies pKa
BHIS592electrostatic stabiliser, modifies pKa, proton acceptor, proton donor, proton relay
site_idMCSA3
Number of Residues4
DetailsM-CSA 646
ChainResidueDetails
CLYS266electrostatic stabiliser, proton acceptor, proton donor, proton relay
CHIS267electrostatic stabiliser, proton acceptor, proton donor, proton relay
CASN431electrostatic stabiliser, modifies pKa
CHIS592electrostatic stabiliser, modifies pKa, proton acceptor, proton donor, proton relay
site_idMCSA4
Number of Residues4
DetailsM-CSA 646
ChainResidueDetails
DLYS266electrostatic stabiliser, proton acceptor, proton donor, proton relay
DHIS267electrostatic stabiliser, proton acceptor, proton donor, proton relay
DASN431electrostatic stabiliser, modifies pKa
DHIS592electrostatic stabiliser, modifies pKa, proton acceptor, proton donor, proton relay

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PDB entries from 2026-03-11

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