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1NF7

Ternary complex of the human type II Inosine Monophosphate Dedhydrogenase with Ribavirin Monophosphate and C2-Mycophenolic Adenine Dinucleotide

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003677molecular_functionDNA binding
A0003723molecular_functionRNA binding
A0003824molecular_functioncatalytic activity
A0003938molecular_functionIMP dehydrogenase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005778cellular_componentperoxisomal membrane
A0005829cellular_componentcytosol
A0006164biological_processpurine nucleotide biosynthetic process
A0006177biological_processGMP biosynthetic process
A0006183biological_processGTP biosynthetic process
A0007623biological_processcircadian rhythm
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0034774cellular_componentsecretory granule lumen
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
A0097294biological_process'de novo' XMP biosynthetic process
A1904813cellular_componentficolin-1-rich granule lumen
B0000166molecular_functionnucleotide binding
B0003677molecular_functionDNA binding
B0003723molecular_functionRNA binding
B0003824molecular_functioncatalytic activity
B0003938molecular_functionIMP dehydrogenase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005778cellular_componentperoxisomal membrane
B0005829cellular_componentcytosol
B0006164biological_processpurine nucleotide biosynthetic process
B0006177biological_processGMP biosynthetic process
B0006183biological_processGTP biosynthetic process
B0007623biological_processcircadian rhythm
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0034774cellular_componentsecretory granule lumen
B0046872molecular_functionmetal ion binding
B0070062cellular_componentextracellular exosome
B0097294biological_process'de novo' XMP biosynthetic process
B1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE K B 901
ChainResidue
BGLY326
BGLY328
BCYS331
BGLU500
BGLY501
BGLY502
BHOH947

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A 902
ChainResidue
ACYS331
AGLU500
AGLY501
AGLY502
AGLY326
AGLY328

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE RVP A 600
ChainResidue
ASER68
AMET70
AASN303
AARG322
AGLY328
ASER329
AILE330
ACYS331
AASP364
AGLY365
AGLY366
AGLY387
ASER388
ATYR411
AGLY413
AMET414
AGLY415
AGLN441
AGLY442
AMYD701
AHOH907
AHOH942

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE MYD A 701
ChainResidue
ATHR252
AHIS253
AASP274
ASER275
ASER276
APHE282
AASN303
AARG322
AGLY324
AMET325
AGLY326
ACYS331
ATHR333
AGLN441
AGLN469
ARVP600
AHOH941
AHOH948

site_idAC5
Number of Residues24
DetailsBINDING SITE FOR RESIDUE RVP B 601
ChainResidue
BSER68
BMET70
BASN303
BARG322
BGLY328
BSER329
BILE330
BCYS331
BASP364
BGLY365
BGLY366
BGLY387
BSER388
BTYR411
BGLY413
BMET414
BGLY415
BGLN441
BGLY442
BMYD702
BHOH918
BHOH919
BHOH922
BHOH939

site_idAC6
Number of Residues19
DetailsBINDING SITE FOR RESIDUE MYD B 702
ChainResidue
BTHR252
BASP274
BSER275
BSER276
BPHE282
BASN303
BARG322
BGLY324
BMET325
BGLY326
BCYS331
BTHR333
BGLN441
BGLN469
BRVP601
BHOH922
BHOH938
BHOH942
BHOH948

Functional Information from PROSITE/UniProt
site_idPS00487
Number of Residues13
DetailsIMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. LRVGMGsGSICiT
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"},{"source":"PubMed","id":"10097070","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues22
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03156","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_03156","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2002","submissionDatabase":"PDB data bank","title":"Crystal structure of human inosine monophosphate dehydrogenase type II complexed with the MPA/NAD analog C2-MAD.","authors":["Risal D.","Strickler M.D.","Goldstein B.M."]}}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues8
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qpr
ChainResidueDetails
AGLU170

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qpr
ChainResidueDetails
BGLU170

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PDB entries from 2025-12-10

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