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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
A0046872molecular_functionmetal ion binding
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
B0046872molecular_functionmetal ion binding
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
DetailsACT_SITE: Thioimidate intermediate => ECO:0000255|HAMAP-Rule:MF_03156
ChainResidueDetails
ACYS331
BCYS331

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03156
ChainResidueDetails
AARG429
BARG429

site_idSWS_FT_FI3
Number of Residues14
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03156
ChainResidueDetails
AASP274
BTYR411
BGLN441
BGLU500
BGLY501
BGLY502
AGLY324
ATYR411
AGLN441
AGLU500
AGLY501
AGLY502
BASP274
BGLY324

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_03156
ChainResidueDetails
AGLY326
AGLY328
ACYS331
BGLY326
BGLY328
BCYS331

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING:
ChainResidueDetails
ASER329
AASP364
AGLY387
BSER329
BASP364
BGLY387

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER160
BSER160

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P50096
ChainResidueDetails
AARG341
AARG355
BARG341
BARG355

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PDB entries from 2024-09-04

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