2o7m

The C-terminal loop of the homing endonuclease I-CreI is essential for DNA binding and cleavage. Identification of a novel site for specificity engineering in the I-CreI scaffold

Method: X-RAY DIFFRACTION Dmax: 85.3 Å Quality: GOOD

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

DNA endonuclease I-CreI

Chlamydomonas reinhardtii

UniProt P05725

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–156 Chain B; UniProt 1–156 Fragment:residues 1-156 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.00 Å R-free 0.235

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.

27 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DNE1_CHLRE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–156; UniProt 1–156 Author chain B; PDBConstruct 1–156; UniProt 1–156

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 2o7m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2o7m
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2o7m
Deposition date deposition_date2006-12-11
Structure title titleThe C-terminal loop of the homing endonuclease I-CreI is essential for DNA binding and cleavage. Identification of a novel site for specificity engineering in the I-CreI scaffold
Keywords keywordsHoming endonuclease, DNA, hydrolase; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.01
Radius of gyration Rg (electron density) rg_electron23.27
Forward intensity I(0) i019489100.00
Molecular weight molecular_weight35135.0 kDa
Excluded volume excluded_volume44760 ų
Envelope volume envelope_volume56331 ų
Hydration-shell volume shell_volume21444 ų
Envelope diameter envelope_diameter84.5
Shell Rg shell_rg29.36
Envelope Rg envelope_rg23.40
Shape Rg shape_rg23.23
Total Rg total_rg24.21
Total atoms total_atoms2484
Residues n_residues306
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 dmax85.3
Rg (real space) rg_real24.12
Rg uncertainty (real space) rg_real_error0.91
I(0) (real space) i0_real1.9490e+07
I(0) uncertainty (real space) i0_real_error2.6810e+05
Rg (reciprocal space) rg_reciprocal24.10
I(0) (reciprocal space) i0_reciprocal19490000.0000
Solution quality estimate total_estimate0.7639
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary26.7
Skewness Skewness skewness0.494
Kurtosis Kurtosis kurtosis-0.104
Angular range angular_range— – 0.3300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2572000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.686; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.871; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2o7ma_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.95 — Homing endonuclease-like
Superfamily Superfamily superfamilyd.95.2 — Homing endonucleases
Family Family familyd.95.2.1 — Group I mobile intron endonuclease
Domain ID domain_idd2o7mb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.95 — Homing endonuclease-like
Superfamily Superfamily superfamilyd.95.2 — Homing endonucleases
Family Family familyd.95.2.1 — Group I mobile intron endonuclease

CATH v4.4 (2 domains)

Domain ID domain_id2o7mA00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology28 — Endonuclease I-creI
Homologous superfamily homologous superfamily10 — Homing endonucleases
Domain ID domain_id2o7mB00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology28 — Endonuclease I-creI
Homologous superfamily homologous superfamily10 — Homing endonucleases

8. Citations (1)

9. Files and Curves (10)