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2CVW

Structures of Yeast Ribonucleotide Reductase I

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005971cellular_componentribonucleoside-diphosphate reductase complex
A0009263biological_processdeoxyribonucleotide biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A 2001
ChainResidue
ASER227
ATTP1001

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE TTP A 1001
ChainResidue
AALA263
AASN270
ATYR285
AVAL286
AASP287
AGLN288
AGLY289
AMG2001
AHOH2046
AHOH2061
AASP226
ASER227
AILE228
AILE231
ALYS243
AARG256
AILE262

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE GDP A 1002
ChainResidue
ASER202
ASER217
ACYS218
AGLY246
AGLY247
AASN426
ALEU427
ACYS428
AGLU430
ALEU445
AMET606
APRO607
ATHR608
AALA609
ASER610
ATHR611
AHOH2002
AHOH2053
AHOH2065
AHOH2123
AHOH2125

Functional Information from PROSITE/UniProt
site_idPS00089
Number of Residues23
DetailsRIBORED_LARGE Ribonucleotide reductase large subunit signature. WdtLrkdimkhGVRNsltMApmP
ChainResidueDetails
ATRP585-PRO607

site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ISQkTIINMAADRSVyI
ChainResidueDetails
AILE690-ILE706

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Cysteine radical intermediate"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P23921","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Important for hydrogen atom transfer","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Important for electron transfer","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 3r1r
ChainResidueDetails
ACYS428
AASN426
ACYS218
AGLU430
ACYS443

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PDB entries from 2025-07-30

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