Loading
PDBj
English日本語简体中文繁體中文한국어
✖
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help
SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9DB2

Class Ia ribonucleotide reductase with mechanism-based inhibitor N3CDP

This is a non-PDB format compatible entry.
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
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0005971cellular_componentribonucleoside-diphosphate reductase complex
B0006457biological_processprotein folding
B0009185biological_processribonucleoside diphosphate metabolic process
B0009263biological_processdeoxyribonucleotide biosynthetic process
B0009265biological_process2'-deoxyribonucleotide biosynthetic process
B0015949biological_processnucleobase-containing small molecule interconversion
B0016491molecular_functionoxidoreductase activity
B0042802molecular_functionidentical protein binding
B0044183molecular_functionprotein folding chaperone
C0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
C0005506molecular_functioniron ion binding
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005971cellular_componentribonucleoside-diphosphate reductase complex
C0009185biological_processribonucleoside diphosphate metabolic process
C0009263biological_processdeoxyribonucleotide biosynthetic process
C0009265biological_process2'-deoxyribonucleotide biosynthetic process
C0015949biological_processnucleobase-containing small molecule interconversion
C0016491molecular_functionoxidoreductase activity
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
D0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
D0005506molecular_functioniron ion binding
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005971cellular_componentribonucleoside-diphosphate reductase complex
D0009185biological_processribonucleoside diphosphate metabolic process
D0009263biological_processdeoxyribonucleotide biosynthetic process
D0009265biological_process2'-deoxyribonucleotide biosynthetic process
D0015949biological_processnucleobase-containing small molecule interconversion
D0016491molecular_functionoxidoreductase activity
D0042802molecular_functionidentical protein binding
D0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00089
Number of Residues23
DetailsRIBORED_LARGE Ribonucleotide reductase large subunit signature. WeaLresikthGLRNstlSAlmP
ChainResidueDetails
ATRP599-PRO621
site_idPS00368
Number of Residues17
DetailsRIBORED_SMALL Ribonucleotide reductase small subunit signature. SEt.IHSrSYthIirnIV
ChainResidueDetails
CSER114-VAL130
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Cysteine radical intermediate"}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9309223","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3R1R","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9309223","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4R1R","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsSite: {"description":"Important for hydrogen atom transfer"}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsSite: {"description":"Important for electron transfer"}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues90
DetailsDomain: {"description":"ATP-cone","evidences":[{"source":"PROSITE-ProRule","id":"PRU00492","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsActive site: {}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues12
DetailsBinding site: {}
ChainResidueDetails
Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 918
ChainResidueDetails
CTYR122pi-pi interaction, single electron relay
CASP237
ACYS439hydrogen radical acceptor, hydrogen radical donor, single electron acceptor
AGLU441proton acceptor
ACYS462
ATYR730pi-pi interaction, single electron relay
ATYR731pi-pi interaction, single electron relay
site_idMCSA2
Number of Residues2
DetailsM-CSA 918
ChainResidueDetails
DTYR122pi-pi interaction, single electron relay
DASP237
BCYS439hydrogen radical acceptor, hydrogen radical donor, single electron acceptor
BGLU441proton acceptor
BCYS462
BTYR730pi-pi interaction, single electron relay
BTYR731pi-pi interaction, single electron relay

243083

PDB entries from 2025-10-15

PDB statisticsPDBj update infoContact PDBjnumon