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1RLR

STRUCTURE OF RIBONUCLEOTIDE REDUCTASE PROTEIN R1

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
A0005829cellular_componentcytosol
A0005971cellular_componentribonucleoside-diphosphate reductase complex
A0006457biological_processprotein folding
A0009185biological_processribonucleoside diphosphate metabolic process
A0009263biological_processdeoxyribonucleotide biosynthetic process
A0009265biological_process2'-deoxyribonucleotide biosynthetic process
A0015949biological_processnucleobase-containing small molecule interconversion
A0016491molecular_functionoxidoreductase activity
A0042802molecular_functionidentical protein binding
A0044183molecular_functionprotein folding chaperone
Functional Information from PROSITE/UniProt
site_idPS00089
Number of Residues23
DetailsRIBORED_LARGE Ribonucleotide reductase large subunit signature. WeaLresikthGLRNstlSAlmP
ChainResidueDetails
ATRP599-PRO621

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 Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9309223","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3R1R","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9309223","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4R1R","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Important for hydrogen atom transfer"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsSite: {"description":"Important for electron transfer"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 3r1r
ChainResidueDetails
AGLU441
ACYS462
ACYS439
ACYS225
AASN437

site_idMCSA1
Number of Residues7
DetailsM-CSA 918
ChainResidueDetails
ACYS225proton donor
AASN437
ACYS439hydrogen radical acceptor, hydrogen radical donor, single electron acceptor
AGLU441proton acceptor
ACYS462
ATYR730pi-pi interaction, single electron relay
ATYR731pi-pi interaction, single electron relay

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PDB entries from 2025-12-24

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