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1SMS

Structure of the Ribonucleotide Reductase Rnr4 Homodimer from Saccharomyces cerevisiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005971cellular_componentribonucleoside-diphosphate reductase complex
A0009263biological_processdeoxyribonucleotide biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0046982molecular_functionprotein heterodimerization activity
B0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005971cellular_componentribonucleoside-diphosphate reductase complex
B0009263biological_processdeoxyribonucleotide biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0046982molecular_functionprotein heterodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE HG A 501
ChainResidue
ATYR194
ACYS217

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE HG A 502
ChainResidue
ACYS228

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE HG B 503
ChainResidue
BTYR194
BCYS217

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE HG B 504
ChainResidue
BCYS228

Functional Information from PROSITE/UniProt
site_idPS00368
Number of Residues17
DetailsRIBORED_SMALL Ribonucleotide reductase small subunit signature. MEn.IYSeVYsmMvdaFF
ChainResidueDetails
AMET123-PHE139

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10014","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1xik
ChainResidueDetails
ATYR131

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1xik
ChainResidueDetails
BTYR131

246031

PDB entries from 2025-12-10

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