2x0x

Ribonucleotide reductase R1 subunit of E. coli to 2.3 A resolution

Method: X-RAY DIFFRACTION

1. Protein Identity and Related Structures Protein Identity & Related Structures

RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE 1 SUBUNIT ALPHA

ESCHERICHIA COLI

UniProt P00452

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 12 RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE 1 SUBUNIT BETA × 6 (P69924) SULFATE ION × 6 water × 12 Consistent with protein count
2 Protein heterocomplex Heteromer Protein 12 RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE 1 SUBUNIT BETA × 6 (P69924) SULFATE ION × 6 water × 12 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name RIR1_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–761; UniProt 1–761 Author chain B; PDBConstruct 1–761; UniProt 1–761 Author chain C; PDBConstruct 1–761; UniProt 1–761

RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE 1 SUBUNIT BETA

OrganismNot specified

UniProt P69924

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 12 RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE 1 SUBUNIT ALPHA × 6 (P00452) SULFATE ION × 6 water × 12 Consistent with protein count
2 Protein heterocomplex Heteromer Protein 12 RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE 1 SUBUNIT ALPHA × 6 (P00452) SULFATE ION × 6 water × 12 Consistent with protein count
3 Protein monomer Monomer Protein 1 water × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name RIR2_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–20; UniProt 357–376 Author chain E; PDBConstruct 1–20; UniProt 357–376 Author chain F; PDBConstruct 1–20; UniProt 357–376 Author chain P; PDBConstruct 1–20; UniProt 357–376

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

2. Structure Basics 2. Structure Basics

Entry ID entry_id2x0x
Deposition date deposition_date2009-12-18
Structure title titleRibonucleotide reductase R1 subunit of E. coli to 2.3 A resolution
Keywords keywordsOXIDOREDUCTASE, NUCLEOTIDE-BINDING, ALTERNATIVE INITIATION, DNA REPLICATION, ALLOSTERIC ENZYME; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

2x0x__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

2x0x__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 109 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

2x0x__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)53.04 Å
Rg (electron density)52.38 Å
Total Rg52.50 Å
Atom count35628
Residues4464
Excluded volume632740 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 2x0x__assembly_1__model_1 dodecameric (12) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 2x0x__assembly_2__model_1 dodecameric (12) Success 4.1.3-1-20251215 (887e7ef) View Download
3 1 2x0x__assembly_3__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download

4. Crystallography and Experiment 4. Crystallography & Experiment

5. Entities and Polymers Entities & Polymers (4)

6. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id2x0xA02
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology70 — Anaerobic Ribonucleotide-triphosphate Reductase Large Chain
Homologous superfamily homologous superfamily20
Domain ID domain_id2x0xB02
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology70 — Anaerobic Ribonucleotide-triphosphate Reductase Large Chain
Homologous superfamily homologous superfamily20
Domain ID domain_id2x0xC02
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology70 — Anaerobic Ribonucleotide-triphosphate Reductase Large Chain
Homologous superfamily homologous superfamily20

7. Citations (2)