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1XSM

PROTEIN R2 OF RIBONUCLEOTIDE REDUCTASE FROM MOUSE

Functional Information from GO Data
ChainGOidnamespacecontents
A0001824biological_processblastocyst development
A0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005971cellular_componentribonucleoside-diphosphate reductase complex
A0008199molecular_functionferric iron binding
A0009185biological_processribonucleoside diphosphate metabolic process
A0009262biological_processdeoxyribonucleotide metabolic process
A0009263biological_processdeoxyribonucleotide biosynthetic process
A0009265biological_process2'-deoxyribonucleotide biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A0051290biological_processprotein heterotetramerization
A1900087biological_processpositive regulation of G1/S transition of mitotic cell cycle
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE A 401
ChainResidue
AGLU170
AGLU233
AGLU267
AHIS270

Functional Information from PROSITE/UniProt
site_idPS00368
Number of Residues17
DetailsRIBORED_SMALL Ribonucleotide reductase small subunit signature. MEn.IHSeMYslLidtYI
ChainResidueDetails
AMET169-ILE185

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10014","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1xik
ChainResidueDetails
ATYR177

240971

PDB entries from 2025-08-27

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