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1JCN

BINARY COMPLEX OF HUMAN TYPE-I INOSINE MONOPHOSPHATE DEHYDROGENASE WITH 6-CL-IMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003676molecular_functionnucleic acid binding
A0003677molecular_functionDNA binding
A0003723molecular_functionRNA binding
A0003824molecular_functioncatalytic activity
A0003938molecular_functionIMP dehydrogenase activity
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006164biological_processpurine nucleotide biosynthetic process
A0006177biological_processGMP biosynthetic process
A0006183biological_processGTP biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0034774cellular_componentsecretory granule lumen
A0035578cellular_componentazurophil granule lumen
A0046651biological_processlymphocyte proliferation
A0046872molecular_functionmetal ion binding
A0097294biological_process'de novo' XMP biosynthetic process
A1904813cellular_componentficolin-1-rich granule lumen
B0000166molecular_functionnucleotide binding
B0003676molecular_functionnucleic acid binding
B0003677molecular_functionDNA binding
B0003723molecular_functionRNA binding
B0003824molecular_functioncatalytic activity
B0003938molecular_functionIMP dehydrogenase activity
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006164biological_processpurine nucleotide biosynthetic process
B0006177biological_processGMP biosynthetic process
B0006183biological_processGTP biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0034774cellular_componentsecretory granule lumen
B0035578cellular_componentazurophil granule lumen
B0046651biological_processlymphocyte proliferation
B0046872molecular_functionmetal ion binding
B0097294biological_process'de novo' XMP biosynthetic process
B1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE CPR A 631
ChainResidue
ASER68
AMET385
AGLY387
ASER388
AHOH676
AHOH698
AHOH734
AHOH748
AARG322
AGLY328
ASER329
ACYS331
AGLN334
AASP364
AGLY365
AGLY366

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE CPR B 631
ChainResidue
BSER68
BMET70
BARG322
BGLY328
BSER329
BCYS331
BGLN334
BASP364
BGLY365
BGLY366
BMET385
BGLY387
BSER388
BHOH639
BHOH689
BHOH698
BHOH716
BHOH734

Functional Information from PROSITE/UniProt
site_idPS00487
Number of Residues13
DetailsIMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. LRVGMGcGSICiT
ChainResidueDetails
ALEU321-THR333

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Thioimidate intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_03156","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03156","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_03156","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"P50096","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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