1u0d

Y33H Mutant of Homing endonuclease I-CreI

Method: X-RAY DIFFRACTION Dmax: 88.9 Å Quality: REASONABLE

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–DNA Homooligomer Protein × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain A; UniProt 1–163 Chain B; UniProt 1–163 Not recorded 5'-D(*GP*CP*GP*AP*AP*AP*CP*GP*TP*CP*GP*TP*GP*AP*GP*AP*CP*AP*GP*TP*TP*CP*CP*G)-3' × 1 5'-D(*CP*GP*GP*AP*AP*CP*TP*GP*TP*CP*TP*CP*AP*CP*GP*AP*CP*GP*TP*TP*TP*CP*GP*C)-3' × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.90 Å R-free 0.257

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 3
Chains and sequence ranges Author chain A; PDBConstruct 1–163; UniProt 1–163 Author chain B; PDBConstruct 1–163; UniProt 1–163

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 1u0d

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1u0d
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1u0d
Deposition date deposition_date2004-07-13
Structure title titleY33H Mutant of Homing endonuclease I-CreI
Keywords keywordsDNA endonuclease I-CreI, PROTEIN/dna, 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_guinier24.73
Radius of gyration Rg (electron density) rg_electron24.41
Forward intensity I(0) i0200928000.00
Molecular weight molecular_weight99321.0 kDa
Excluded volume excluded_volume117340 ų
Envelope volume envelope_volume73415 ų
Hydration-shell volume shell_volume25886 ų
Envelope diameter envelope_diameter89.0
Shell Rg shell_rg31.25
Envelope Rg envelope_rg25.07
Shape Rg shape_rg24.36
Total Rg total_rg24.87
Total atoms total_atoms6892
Residues n_residues704
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 dmax88.9
Rg (real space) rg_real24.95
Rg uncertainty (real space) rg_real_error0.80
I(0) (real space) i0_real2.0090e+08
I(0) uncertainty (real space) i0_real_error3.0490e+06
Rg (reciprocal space) rg_reciprocal24.90
I(0) (reciprocal space) i0_reciprocal200900000.0000
Solution quality estimate total_estimate0.6601
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.4
Skewness Skewness skewness0.571
Kurtosis Kurtosis kurtosis-0.164
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6128000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.625; Stabil: 1.000; Sysdev: 0.338; Positv: 1.000; Valcen: 0.692; Smooth: 0.996

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_idd1u0da_
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_idd1u0db_
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_id1u0dA00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology28 — Endonuclease I-creI
Homologous superfamily homologous superfamily10 — Homing endonucleases
Domain ID domain_id1u0dB00
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)