Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

9HFQ

Cryo-EM structure of human CDADC1 inactive mutant (E400A): trimer without a ligand

Functional Information from GO Data
ChainGOidnamespacecontents
A0004126molecular_functioncytidine deaminase activity
A0004132molecular_functiondCMP deaminase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0006229biological_processdUTP biosynthetic process
A0008270molecular_functionzinc ion binding
A0008829molecular_functiondCTP deaminase activity
A0042803molecular_functionprotein homodimerization activity
A0061676molecular_functionimportin-alpha family protein binding
A0070207biological_processprotein homotrimerization
A0070383biological_processDNA cytosine deamination
B0004126molecular_functioncytidine deaminase activity
B0004132molecular_functiondCMP deaminase activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0006229biological_processdUTP biosynthetic process
B0008270molecular_functionzinc ion binding
B0008829molecular_functiondCTP deaminase activity
B0042803molecular_functionprotein homodimerization activity
B0061676molecular_functionimportin-alpha family protein binding
B0070207biological_processprotein homotrimerization
B0070383biological_processDNA cytosine deamination
C0004126molecular_functioncytidine deaminase activity
C0004132molecular_functiondCMP deaminase activity
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0006229biological_processdUTP biosynthetic process
C0008270molecular_functionzinc ion binding
C0008829molecular_functiondCTP deaminase activity
C0042803molecular_functionprotein homodimerization activity
C0061676molecular_functionimportin-alpha family protein binding
C0070207biological_processprotein homotrimerization
C0070383biological_processDNA cytosine deamination
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues36
DetailsMotif: {"description":"Nuclear export signal","evidences":[{"source":"PubMed","id":"26945630","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01083","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"40324085","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01083","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"40324085","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"9HFQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"9HFR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"9HFS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"9HFT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"40324085","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"9HFQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"9HFR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"9HFS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"9HFT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues30
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"40324085","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"9HFS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

256789

PDB entries from 2026-07-22

PDB statisticsPDBj update infoContact PDBjnumon