Structure of PDB 1jcn Chain B

Receptor sequence
>1jcnB (length=395) Species: 9606 (Homo sapiens) [Search protein sequence]
TGYVPEDGLTAQQLFASADDLTYNDFLILPGFIDFIADEVDLTSALTRKI
TLKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNCTPEFQANEVRKVKN
FEQGFITDPVVLSPGIPITEVGIVTSRDIDPRIELVVAPAGVTLKEANEI
LQRSKKGKLPIVNDCDELVRTDLKKNRDYPLASKDSQKQLLCGAAVGTRE
DDKYRLDLLTQAGVDVIVLDSSQGNSVYQIAMVHYIKQKYPHLQVIGGNV
VTAAQAKNLIDAGVDGLRVGMGCGSICITQEVMACGRPQGTAVYKVAEYA
RRFGVPIIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEKGSIQ
KFVPYLIAGIQHGCQDIGARSLSVLRSMMYSGELKFEKRTMSAQI
3D structure
PDB1jcn Crystal Structure of the Human Type I Inosine Monophosphate Dehydrogenase and Implications for Isoform Specificity
ChainB
Resolution2.5 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.1.1.205: IMP dehydrogenase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CPR B S68 M70 R322 G328 S329 C331 Q334 D364 G387 S388 S59 M61 R268 G274 S275 C277 Q280 D310 G333 S334
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003676 nucleic acid binding
GO:0003677 DNA binding
GO:0003723 RNA binding
GO:0003824 catalytic activity
GO:0003938 IMP dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
Biological Process
GO:0006164 purine nucleotide biosynthetic process
GO:0006177 GMP biosynthetic process
GO:0006183 GTP biosynthetic process
Cellular Component
GO:0005576 extracellular region
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0034774 secretory granule lumen
GO:0035578 azurophil granule lumen
GO:1904813 ficolin-1-rich granule lumen

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1jcn, PDBe:1jcn, PDBj:1jcn
PDBsum1jcn
PubMed
UniProtP20839|IMDH1_HUMAN Inosine-5'-monophosphate dehydrogenase 1 (Gene Name=IMPDH1)

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