7afs

The structure of Artemis variant D37A

Method: X-RAY DIFFRACTION Dmax: 78.9 Å Quality: GOOD

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

Protein artemis

Homo sapiens

UniProt Q96SD1

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 1–361 Mutation:D37A NI NICKEL (II) ION × 1 ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;277.15 K;0.2 M Ammonium Acetate, 0.1 M Bis-TRIS pH 5.5, 25% PEG 3350 Resolution 1.70 Å R-free 0.216

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.

13 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DCR1C_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–362; UniProt 1–361

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 7afs

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7afs
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7afs
Deposition date deposition_date2020-09-20
Structure title titleThe structure of Artemis variant D37A
Keywords keywordsArtemis, SNM1C, DCLRE1C, Nuclease, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.22
Radius of gyration Rg (electron density) rg_electron22.19
Forward intensity I(0) i027325400.00
Molecular weight molecular_weight40192.0 kDa
Excluded volume excluded_volume50265 ų
Envelope volume envelope_volume59732 ų
Hydration-shell volume shell_volume22615 ų
Envelope diameter envelope_diameter81.7
Shell Rg shell_rg28.84
Envelope Rg envelope_rg22.43
Shape Rg shape_rg22.21
Total Rg total_rg22.95
Total atoms total_atoms2823
Residues n_residues359
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 dmax78.9
Rg (real space) rg_real23.21
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real2.7330e+07
I(0) uncertainty (real space) i0_real_error3.6800e+05
Rg (reciprocal space) rg_reciprocal23.22
I(0) (reciprocal space) i0_reciprocal27330000.0000
Solution quality estimate total_estimate0.8744
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.3
Skewness Skewness skewness0.344
Kurtosis Kurtosis kurtosis-0.336
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6810000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.821; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.928

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)