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2CVU

Structures of Yeast Ribonucleotide Reductase I

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
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
AANP1001

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ANP A 1001
ChainResidue
ATYR285
AVAL286
AASP287
AMG2001
AHOH2009
AHOH2012
AHOH2052
AASP226
ASER227
AILE228
AILE231
ALYS243
AARG256
AILE262
AALA263

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE CDP A 1002
ChainResidue
AALA201
ASER202
ASER217
ACYS218
AGLY247
AASN426
ALEU427
ACYS428
AGLU430
AMET606
APRO607
ATHR608
AALA609
ATHR611
AHOH2006

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

226707

PDB entries from 2024-10-30

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