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2CVX

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 Residues1
DetailsBINDING SITE FOR RESIDUE MG A 2001
ChainResidue
ADGT1001

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE DGT A 1001
ChainResidue
AASN270
ATYR285
AASP287
AGLY289
AGLY290
AMG2001
AHOH2014
AHOH2017
AHOH2018
AHOH2021
AASP226
AHOH2022
AHOH2097
AHOH2114
ASER227
AILE228
ALYS243
AARG256
AILE262
AALA263
AGLY264

site_idAC3
Number of Residues26
DetailsBINDING SITE FOR RESIDUE ADP A 1002
ChainResidue
AALA201
ASER202
ASER217
ACYS218
AGLY246
AGLY247
AGLN288
AARG293
AALA296
AASN426
ACYS428
AGLU430
ALEU445
AMET606
APRO607
ATHR608
AALA609
ASER610
ATHR611
AHOH2006
AHOH2007
AHOH2010
AHOH2019
AHOH2145
AHOH2164
AHOH2215

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
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AASN426
AGLU430

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Cysteine radical intermediate
ChainResidueDetails
ACYS428

site_idSWS_FT_FI3
Number of Residues13
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P23921
ChainResidueDetails
ALYS5
AALA263
AASN426
AGLU430
ATHR608
AGLU11
ATHR53
AASP57
ASER202
ASER217
AASP226
ALYS243
AARG256

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Important for hydrogen atom transfer => ECO:0000250
ChainResidueDetails
ACYS218
ACYS443

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Important for electron transfer => ECO:0000250
ChainResidueDetails
ATYR741
ATYR742

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Interacts with thioredoxin/glutaredoxin => ECO:0000250
ChainResidueDetails
ACYS883
ACYS886

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ASER227
ASER837

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P21672
ChainResidueDetails
ASER816

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER887

site_idSWS_FT_FI10
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
ChainResidueDetails
ALYS387
ALYS853

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 2025-06-11

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