1q39

Crystal structure of the DNA repair enzyme endonuclease-VIII (Nei) from E. coli: The WT enzyme at 2.8 resolution.

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

Endonuclease VIII

Escherichia coli

UniProt P50465

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 ZINC ION × 1 CALCIUM ION × 3 water × 1 Consistent with protein count
2 Protein homooligomer Homooligomer Protein 4 ZINC ION × 4 CALCIUM ION × 12 water × 4 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name END8_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–262; UniProt 1–262

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_id1q39
Deposition date deposition_date2003-07-29
Structure title titleCrystal structure of the DNA repair enzyme endonuclease-VIII (Nei) from E. coli: The WT enzyme at 2.8 resolution.
Keywords keywordshydrolase; HYDROLASE
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.

1q39__assembly_1__model_1

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

Download this curve (.dat)

1q39__assembly_1__model_1 | I(q)

10-2 10-1 105 106 107 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

1q39__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)22.58 Å
Rg (electron density)21.77 Å
Total Rg22.64 Å
Atom count2030
Residues257
Excluded volume36162 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1q39__assembly_1__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 1q39__assembly_2__model_1 tetrameric (4) 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 (4)

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6. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1q39a1
Class classa — All alpha proteins
Fold Fold folda.156 — S13-like H2TH domain
Superfamily Superfamily superfamilya.156.1 — S13-like H2TH domain
Family Family familya.156.1.2 — Middle domain of MutM-like DNA repair proteins
Domain ID domain_idd1q39a2
Class classb — All beta proteins
Fold Fold foldb.113 — N-terminal domain of MutM-like DNA repair proteins
Superfamily Superfamily superfamilyb.113.1 — N-terminal domain of MutM-like DNA repair proteins
Family Family familyb.113.1.1 — N-terminal domain of MutM-like DNA repair proteins
Domain ID domain_idd1q39a3
Class classg — Small proteins
Fold Fold foldg.39 — Glucocorticoid receptor-like (DNA-binding domain)
Superfamily Superfamily superfamilyg.39.1 — Glucocorticoid receptor-like (DNA-binding domain)
Family Family familyg.39.1.8 — C-terminal, Zn-finger domain of MutM-like DNA repair proteins

CATH v4.4 (2 domains)

Domain ID domain_id1q39A01
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology190 — N-terminal domain of MutM-like DNA repair proteins
Homologous superfamily homologous superfamily10 — MutM-like, N-terminal
Domain ID domain_id1q39A02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily50 —
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7. Citations (1)