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1W69

Crystal Structure of Mouse Ribonucleotide Reductase Subunit R2 under Reducing Conditions. A Fully Occupied Dinuclear Iron Cluster and Bound Acetate.

Functional Information from GO Data
ChainGOidnamespacecontents
A0001824biological_processblastocyst development
A0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005635cellular_componentnuclear envelope
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
A0055086biological_processnucleobase-containing small molecule metabolic process
A1900087biological_processpositive regulation of G1/S transition of mitotic cell cycle
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE2 A1349
ChainResidue
AASP139
AGLU170
AHIS173
AGLU267
AFE21350
AACY1351

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE2 A1350
ChainResidue
AHIS270
AFE21349
AACY1351
AGLU170
AGLU233
AGLU267

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACY A1351
ChainResidue
AASP139
AVAL142
AGLU170
AGLU233
AGLU267
AFE21349
AFE21350

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
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10014
ChainResidueDetails
ATYR177

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AASP139
AGLU170
AHIS173
AGLU233
AGLU267
AHIS270

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079
ChainResidueDetails
ASER20

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:21183079
ChainResidueDetails
ATHR33

220113

PDB entries from 2024-05-22

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