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3S87

Structure of Yeast Ribonucleotide Reductase 1 with dGTP and ADP

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 Residues4
DetailsBINDING SITE FOR RESIDUE MG A 2001
ChainResidue
AHOH958
AHOH986
ADGT1001
AHOH1005

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE DGT A 1001
ChainResidue
AILE262
AALA263
AGLY264
ATYR285
AASP287
AGLY289
AGLY290
AHOH922
AHOH958
AHOH960
AHOH986
AHOH990
AHOH1005
AHOH1070
AHOH1086
AMG2001
AASP226
ASER227
AILE228
ALYS243
AARG256

site_idAC3
Number of Residues24
DetailsBINDING SITE FOR RESIDUE ADP A 1002
ChainResidue
AALA201
ASER202
ASER217
ACYS218
AGLY247
AGLN288
AARG293
AALA296
AASN426
ACYS428
AGLU430
AMET606
APRO607
ATHR608
AALA609
ASER610
ATHR611
AHOH896
AHOH902
AHOH937
AHOH945
AHOH992
AHOH1000
AHOH1053

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

238895

PDB entries from 2025-07-16

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