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Ligands
Code Name Style Show Link
DGT 2'-deoxyguanosine-5'-triphosphate
FE Fe (III) ion
MG Magnesium ion
Non-standard Residues
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Glycosylation
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Code : 2BQ1   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : Ribonucleotide reductase class 1b holocomplex R1E,R2F from Salmonella typhimurium
Release Data : 2006-05-17
Compound :
mol_id molecule chains synonym
1 RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE 2 ALPHA SUBUNIT E,F RIBONUCLEOTIDE REDUCTASE 2, R1E PROTEIN
ec: 1.17.4.1
mol_id molecule chains synonym
2 RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE 2 BETA SUBUNIT I,J RIBONUCLEOTIDE REDUCTASE 2, R2F PROTEIN
ec: 1.17.4.1
Source :
mol_id organism_scientific expression_system
1 SALMONELLA TYPHIMURIUM  (taxid:602) ESCHERICHIA COLI  (taxid:469008)
expression_system_strain: BL21(DE3)
expression_system_plasmid: PET24A
mol_id organism_scientific expression_system
2 SALMONELLA TYPHIMURIUM  (taxid:602) ESCHERICHIA COLI  (taxid:469008)
expression_system_strain: BL21(DE3)
expression_system_vector: PET24A
Authors : Uppsten, M., Farnegardh, M., Domkin, V., Uhlin, U.
Keywords : R1, R2, R1E, R2F, IRON, CLASS 1B, HOLOCOMPLEX, ALLOSTERIC REGULATION, RIBONUCLEOTIDE REDUCTASE, ATP-BINDING, METAL-BINDING, OXIDOREDUCTASE, DNA REPLICATION, RADICAL TRANSFER, ALLOSTERIC ENZYME, ASYMMETRIC COMPLEX, NUCLEOTIDE-BINDING
Exp. method : X-RAY DIFFRACTION ( 3.99 Å )
Citation :

The First Holocomplex Structure of Ribonucleotide Reductase Gives New Insight Into its Mechanism of Action

Uppsten, M.,Farnegardh, M.,Domkin, V.  et al.
(2006)  J.Mol.Biol.  359 : 365

PubMed: 16631785
DOI: 10.1016/J.JMB.2006.03.035

Chain : E, F
UniProt : Q08698 (RIR3_SALTY)
Reaction: EC: Evidence:
Physiological Direction:
[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'- diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'- diphosphate 1.17.4.1 -
-
Chain : I, J
UniProt : P17424 (RIR4_SALTY)
Reaction: EC: Evidence:
Physiological Direction:
[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'- diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'- diphosphate 1.17.4.1 PROSITE-ProRule:PRU10014
-