6r1r

RIBONUCLEOTIDE REDUCTASE E441D MUTANT R1 PROTEIN FROM ESCHERICHIA COLI

Method: X-RAY DIFFRACTION
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1. Protein Identity and Related Structures Protein Identity & Related Structures

RIBONUCLEOTIDE REDUCTASE R1 PROTEIN

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 3 RIBONUCLEOTIDE REDUCTASE R2 PROTEIN × 2 (P69924) water × 1 Consistent with protein count
2 Protein heterocomplex Heteromer Protein 2 RIBONUCLEOTIDE REDUCTASE R2 PROTEIN × 1 (P69924) water × 1 Consistent with protein count
3 Protein heterocomplex Heteromer Protein 2 RIBONUCLEOTIDE REDUCTASE R2 PROTEIN × 1 (P69924) water × 1 Consistent with protein count
4 Protein heterocomplex Heteromer Protein 12 RIBONUCLEOTIDE REDUCTASE R2 PROTEIN × 6 (P69924) water × 6 Consistent with protein count
5 Protein heterocomplex Heteromer Protein 12 RIBONUCLEOTIDE REDUCTASE R2 PROTEIN × 6 (P69924) water × 6 Consistent with protein count
6 Protein homooligomer Homooligomer Protein 6 water × 6 Consistent with protein count
7 Protein heterocomplex Heteromer Protein 4 RIBONUCLEOTIDE REDUCTASE R2 PROTEIN × 2 (P69924) water × 2 Consistent with protein count
8 Protein heterocomplex Heteromer Protein 4 RIBONUCLEOTIDE REDUCTASE R2 PROTEIN × 2 (P69924) water × 2 Consistent with protein count
9 Protein heterocomplex Heteromer Protein 2 RIBONUCLEOTIDE REDUCTASE R2 PROTEIN × 1 (P69924) water × 1 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

RIBONUCLEOTIDE REDUCTASE R2 PROTEIN

Escherichia coli

UniProt P69924

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 3 RIBONUCLEOTIDE REDUCTASE R1 PROTEIN × 1 (P00452) water × 1 Consistent with protein count
2 Protein heterocomplex Heteromer Protein 2 RIBONUCLEOTIDE REDUCTASE R1 PROTEIN × 1 (P00452) water × 1 Consistent with protein count
3 Protein heterocomplex Heteromer Protein 2 RIBONUCLEOTIDE REDUCTASE R1 PROTEIN × 1 (P00452) water × 1 Consistent with protein count
4 Protein heterocomplex Heteromer Protein 12 RIBONUCLEOTIDE REDUCTASE R1 PROTEIN × 6 (P00452) water × 6 Consistent with protein count
5 Protein heterocomplex Heteromer Protein 12 RIBONUCLEOTIDE REDUCTASE R1 PROTEIN × 6 (P00452) water × 6 Consistent with protein count
7 Protein heterocomplex Heteromer Protein 4 RIBONUCLEOTIDE REDUCTASE R1 PROTEIN × 2 (P00452) water × 2 Consistent with protein count
8 Protein heterocomplex Heteromer Protein 4 RIBONUCLEOTIDE REDUCTASE R1 PROTEIN × 2 (P00452) water × 2 Consistent with protein count
9 Protein heterocomplex Heteromer Protein 2 RIBONUCLEOTIDE REDUCTASE R1 PROTEIN × 1 (P00452) 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 356–375 Author chain E; PDBConstruct 1–20; UniProt 356–375 Author chain F; PDBConstruct 1–20; UniProt 356–375 Author chain P; PDBConstruct 1–20; UniProt 356–375

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id6r1r
Deposition date deposition_date1997-09-17
Structure title titleRIBONUCLEOTIDE REDUCTASE E441D MUTANT R1 PROTEIN FROM ESCHERICHIA COLI
Keywords keywords;RIBONUCLEOTIDE REDUCTASE, DEOXYRIBONUCLEOTIDE SYNTHESIS, RADICAL CHEMISTRY, ALLOSTERIC REGULATION, SPECIFICITY, COMPLEX (OXIDOREDUCTASE-PEPTIDE), COMPLEX (OXIDOREDUCTASE-PEPTIDE) complex ;; COMPLEX (OXIDOREDUCTASE/PEPTIDE)
Experimental Method methodX-RAY DIFFRACTION
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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.

6r1r__assembly_3__model_1

Assembly 3 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

6r1r__assembly_3__model_1 | I(q)

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

6r1r__assembly_3__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)28.58 Å
Rg (electron density)27.62 Å
Total Rg28.36 Å
Atom count6014
Residues756
Excluded volume106790 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 6r1r__assembly_1__model_1 trimeric (3) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 6r1r__assembly_2__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
3 1 6r1r__assembly_3__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
4 1 6r1r__assembly_4__model_1 dodecameric (12) Success 4.1.3-1-20251215 (887e7ef) View Download
5 1 6r1r__assembly_5__model_1 dodecameric (12) Success 4.1.3-1-20251215 (887e7ef) View Download
6 1 6r1r__assembly_6__model_1 hexameric (6) Success 4.1.3-1-20251215 (887e7ef) View Download
7 1 6r1r__assembly_7__model_1 tetrameric (4) Success 4.1.3-1-20251215 (887e7ef) View Download
8 1 6r1r__assembly_8__model_1 tetrameric (4) Success 4.1.3-1-20251215 (887e7ef) View Download
9 1 6r1r__assembly_9__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (3)

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6. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd6r1ra1
Class classa — All alpha proteins
Fold Fold folda.98 — R1 subunit of ribonucleotide reductase, N-terminal domain
Superfamily Superfamily superfamilya.98.1 — R1 subunit of ribonucleotide reductase, N-terminal domain
Family Family familya.98.1.1 — R1 subunit of ribonucleotide reductase, N-terminal domain
Domain ID domain_idd6r1ra2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.7 — PFL-like glycyl radical enzymes
Superfamily Superfamily superfamilyc.7.1 — PFL-like glycyl radical enzymes
Family Family familyc.7.1.2 — R1 subunit of ribonucleotide reductase, C-terminal domain
Domain ID domain_idd6r1rb1
Class classa — All alpha proteins
Fold Fold folda.98 — R1 subunit of ribonucleotide reductase, N-terminal domain
Superfamily Superfamily superfamilya.98.1 — R1 subunit of ribonucleotide reductase, N-terminal domain
Family Family familya.98.1.1 — R1 subunit of ribonucleotide reductase, N-terminal domain
Domain ID domain_idd6r1rb2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.7 — PFL-like glycyl radical enzymes
Superfamily Superfamily superfamilyc.7.1 — PFL-like glycyl radical enzymes
Family Family familyc.7.1.2 — R1 subunit of ribonucleotide reductase, C-terminal domain
Domain ID domain_idd6r1rc1
Class classa — All alpha proteins
Fold Fold folda.98 — R1 subunit of ribonucleotide reductase, N-terminal domain
Superfamily Superfamily superfamilya.98.1 — R1 subunit of ribonucleotide reductase, N-terminal domain
Family Family familya.98.1.1 — R1 subunit of ribonucleotide reductase, N-terminal domain
Domain ID domain_idd6r1rc2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.7 — PFL-like glycyl radical enzymes
Superfamily Superfamily superfamilyc.7.1 — PFL-like glycyl radical enzymes
Family Family familyc.7.1.2 — R1 subunit of ribonucleotide reductase, C-terminal domain

CATH v4.4 (3 domains)

Domain ID domain_id6r1rA02
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology70 — Anaerobic Ribonucleotide-triphosphate Reductase Large Chain
Homologous superfamily homologous superfamily20 —
Domain ID domain_id6r1rB02
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology70 — Anaerobic Ribonucleotide-triphosphate Reductase Large Chain
Homologous superfamily homologous superfamily20 —
Domain ID domain_id6r1rC02
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology70 — Anaerobic Ribonucleotide-triphosphate Reductase Large Chain
Homologous superfamily homologous superfamily20 —
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7. Citations (3)