3fbd

Crystal structure of the nuclease domain of COLE7(D493Q mutant) in complex with an 18-BP duplex DNA

Method: X-RAY DIFFRACTION Dmax: 121.0 Å Quality: SUSPICIOUS

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–DNA Monomer Protein × 1 DNA 2 PDB declaration: trimeric(3) Consistent with all polymer counts Chain A; UniProt 445–576 Fragment:NUCLEASE DOMAIN Mutation:D493Q 5'-D(*DGP*DGP*DAP*DAP*DTP*DTP*DCP*DGP*DAP*DTP*DCP*DGP*DAP*DAP*DTP*DTP*DCP*DC)-3' × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;298 K;15% PEG 3350, 16.25% MPD, 0.15M ammonium acetate, 0.025M sodium acetate, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.90 Å R-free 0.264
2 Protein–DNA Monomer Protein × 1 DNA 2 PDB declaration: trimeric(3) Consistent with all polymer counts Chain D; UniProt 445–576 Fragment:NUCLEASE DOMAIN Mutation:D493Q 5'-D(*DGP*DGP*DAP*DAP*DTP*DTP*DCP*DGP*DAP*DTP*DCP*DGP*DAP*DAP*DTP*DTP*DCP*DC)-3' × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;298 K;15% PEG 3350, 16.25% MPD, 0.15M ammonium acetate, 0.025M sodium acetate, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.90 Å R-free 0.264

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 1–132; UniProt 445–576 Author chain D; PDBConstruct 1–132; UniProt 445–576

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 3fbd

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3fbd
Deposition date deposition_date2008-11-19
Structure title titleCrystal structure of the nuclease domain of COLE7(D493Q mutant) in complex with an 18-BP duplex DNA
Keywords keywords;Computational redesign, Protein engineering, Protein-nucleic acid interactions, DNase, DNA hydrolysis., Antibiotic, Antimicrobial, Bacteriocin, Endonuclease, Hydrolase, Metal-binding, Nuclease, Plasmid, Zinc, HYDROLASE-DNA COMPLEX ;; HYDROLASE/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier39.44
Radius of gyration Rg (electron density) rg_electron42.05
Forward intensity I(0) i069215900.00
Molecular weight molecular_weight52256.0 kDa
Excluded volume excluded_volume58878 ų
Envelope volume envelope_volume90614 ų
Hydration-shell volume shell_volume19528 ų
Envelope diameter envelope_diameter130.1
Shell Rg shell_rg42.79
Envelope Rg envelope_rg40.70
Shape Rg shape_rg42.12
Total Rg total_rg41.90
Total atoms total_atoms3592
Residues n_residues335
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 dmax121.0
Rg (real space) rg_real39.75
Rg uncertainty (real space) rg_real_error0.47
I(0) (real space) i0_real6.8340e+07
I(0) uncertainty (real space) i0_real_error1.0320e+06
Rg (reciprocal space) rg_reciprocal39.78
I(0) (reciprocal space) i0_reciprocal69180000.0000
Solution quality estimate total_estimate0.4344
Solution quality rating solution_quality SUSPICIOUS a SUSPICIOUS solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary24.2
Skewness Skewness skewness0.450
Kurtosis Kurtosis kurtosis-0.955
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha1.5840
Highest regularization parameter α highest_alpha2295000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.292; Stabil: 0.895; Sysdev: 0.000; Positv: 1.000; Valcen: 0.080; Smooth: 0.006

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3fbda_
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_idd3fbdd_
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

CATH v4.4 (2 domains)

Domain ID domain_id3fbdA00
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_id3fbdD00
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)