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1JK0

Ribonucleotide reductase Y2Y4 heterodimer

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
A0008198molecular_functionferrous iron binding
A0008270molecular_functionzinc ion binding
A0009263biological_processdeoxyribonucleotide biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
A0046982molecular_functionprotein heterodimerization activity
A0060090molecular_functionmolecular adaptor 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 Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
AGLN172
AGLU176
AGLU239
AGLU273
AHIS276

Functional Information from PROSITE/UniProt
site_idPS00368
Number of Residues17
DetailsRIBORED_SMALL Ribonucleotide reductase small subunit signature. IEn.IHSeTYslLidtYI
ChainResidueDetails
AILE175-ILE191
BMET123-PHE139

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10014
ChainResidueDetails
BTYR131

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0000269|Ref.5, ECO:0007744|PubMed:22814378
ChainResidueDetails
BMET1
AGLU176
AHIS179
AGLU239
AGLU273
AHIS276

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:18407956
ChainResidueDetails
BSER169

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198
ChainResidueDetails
BSER332
BSER336

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19779198
ChainResidueDetails
BTHR334

site_idSWS_FT_FI6
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
ChainResidueDetails
BLYS337

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1xik
ChainResidueDetails
ATYR183

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

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PDB entries from 2025-06-11

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