3zfk

N-terminal truncated Nuclease Domain of Colicin E7

Method: X-RAY DIFFRACTION Dmax: 79.7 Å Quality: REASONABLE

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

COLICIN-E7

ESCHERICHIA COLI

UniProt Q47112

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 450–573 Fragment:COLICIN E7 METALLONUCLEASE DOMAIN, RESIDUES 450-573 ZN ZINC ION × 1 CL CHLORIDE ION × 1 SO4 SULFATE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.5;0.1 M LITHIUM SULFATE, 50 MM SODIUM ACETATE PH 4.5, 25 % W/V PEG 400 Resolution 1.70 Å R-free 0.234
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 450–573 Fragment:COLICIN E7 METALLONUCLEASE DOMAIN, RESIDUES 450-573 ZN ZINC ION × 1 CL CHLORIDE ION × 1 SO4 SULFATE ION × 4 ACT ACETATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.5;0.1 M LITHIUM SULFATE, 50 MM SODIUM ACETATE PH 4.5, 25 % W/V PEG 400 Resolution 1.70 Å R-free 0.234

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

16 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CEA7_ECOLX
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 9–132; UniProt 450–573 Author chain B; PDBConstruct 9–132; UniProt 450–573

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.

SAXS scattering curve SAXS Profile

SAXS profile for 3zfk

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3zfk
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3zfk
Deposition date deposition_date2012-12-11
Structure title titleN-terminal truncated Nuclease Domain of Colicin E7
Keywords keywordsHYDROLASE, ARTIFICIAL METALLONUCLEASE, ALLOSTERIC CONTROL; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier23.06
Radius of gyration Rg (electron density) rg_electron22.72
Forward intensity I(0) i018659300.00
Molecular weight molecular_weight30085.0 kDa
Excluded volume excluded_volume36554 ų
Envelope volume envelope_volume45467 ų
Hydration-shell volume shell_volume18226 ų
Envelope diameter envelope_diameter80.4
Shell Rg shell_rg27.92
Envelope Rg envelope_rg22.77
Shape Rg shape_rg22.69
Total Rg total_rg23.45
Total atoms total_atoms4110
Residues n_residues256
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax79.7
Rg (real space) rg_real23.28
Rg uncertainty (real space) rg_real_error0.57
I(0) (real space) i0_real1.8660e+07
I(0) uncertainty (real space) i0_real_error2.8860e+05
Rg (reciprocal space) rg_reciprocal23.23
I(0) (reciprocal space) i0_reciprocal18660000.0000
Solution quality estimate total_estimate0.6205
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.1
Skewness Skewness skewness0.559
Kurtosis Kurtosis kurtosis-0.318
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4129000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.613; Stabil: 1.000; Sysdev: 0.171; Positv: 1.000; Valcen: 0.732; Smooth: 0.977

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd3zfka1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.4 — His-Me finger endonucleases
Superfamily Superfamily superfamilyd.4.1 — His-Me finger endonucleases
Family Family familyd.4.1.1 — HNH-motif
Domain ID domain_idd3zfka2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd3zfkb1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.4 — His-Me finger endonucleases
Superfamily Superfamily superfamilyd.4.1 — His-Me finger endonucleases
Family Family familyd.4.1.1 — HNH-motif
Domain ID domain_idd3zfkb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id3zfkA00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology540 — Colicin E7 immunity protein; Chain B, fragment: Endonuclease domain
Homologous superfamily homologous superfamily10 — Colicin/pyocin, DNase domain
Domain ID domain_id3zfkB00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology540 — Colicin E7 immunity protein; Chain B, fragment: Endonuclease domain
Homologous superfamily homologous superfamily10 — Colicin/pyocin, DNase domain

8. Citations (1)

9. Files and Curves (10)