1RLR

STRUCTURE OF RIBONUCLEOTIDE REDUCTASE PROTEIN R1

PDB DOI: https://doi.org/10.2210/pdb1RLR/pdb

Classification: OXIDOREDUCTASE
Organism(s): Escherichia coli
Expression System: Escherichia coli
Mutation(s): No

Deposited: 1994-08-12 Released: 1996-12-23
Deposition Author(s): Uhlin, U., Eklund, H.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.50 Å
R-Value Work: 0.210
R-Value Observed: 0.210

wwPDB Validation 3D Report Full Report

This is version 1.2 of the entry. See complete history.

Literature

Structure of ribonucleotide reductase protein R1.

Uhlin, U., Eklund, H.

(1994) Nature 370: 533-539

PubMed: 8052308 Search on PubMed
DOI: https://doi.org/10.1038/370533a0
Primary Citation of Related Structures:
1RLR

PubMed Abstract:
Ribonucleotide reductase is the only enzyme that catalyses de novo formation of deoxyribonucleotides and is thus a key enzyme in DNA synthesis. The radical-based reaction involves five cysteins. Two redox-active cysteines are located at adjacent antiparallel strands in a new type of ten-stranded alpha/beta-barrel, and two others at the carboxyl end in a flexible arm. The fifth cysteine, in a loop in the centre of the barrel, is positioned to initiate the radical reaction.

Organizational Affiliation

Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala.

Macromolecule Content

Total Structure Weight: 86.01 kDa
Atom Count: 5,875
Modelled Residue Count: 737
Deposited Residue Count: 761
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
RIBONUCLEOTIDE REDUCTASE PROTEIN R1	A	761	Escherichia coli	Mutation(s): 0 EC: 1.17.4.1
UniProt
Find proteins for P00452 (Escherichia coli (strain K12)) Explore P00452 Go to UniProtKB: P00452
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P00452
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.50 Å
R-Value Work: 0.210
R-Value Observed: 0.210
Space Group: H 3 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 226	α = 90
b = 226	β = 90
c = 341	γ = 120

Software Package:

Software Name	Purpose
X-PLOR	model building
X-PLOR	refinement
X-PLOR	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 1996-12-23

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 1996-12-23
Type: Initial release
Version 1.1: 2008-03-24
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.