7rgw

Crystal structure of HERC2 DOC domain

Method: X-RAY DIFFRACTION Dmax: 52.5 Å Quality: GOOD

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

E3 ubiquitin-protein ligase HERC2

Homo sapiens

UniProt O95714

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 2759–2914 Fragment:DOC domain (UNP residues 2759-2914) PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277.15 K;0.1 M HEPES, pH 7.5, 25% PEG3350 Resolution 1.99 Å R-free 0.213

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.

14 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HERC2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 19–174; UniProt 2759–2914

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 7rgw

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7rgw
Deposition date deposition_date2021-07-15
Structure title titleCrystal structure of HERC2 DOC domain
Keywords keywordsDOC domain of E3 ubiquitin ligase HERC2, CELL CYCLE; CELL CYCLE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.05
Radius of gyration Rg (electron density) rg_electron14.62
Forward intensity I(0) i04907820.00
Molecular weight molecular_weight15779.0 kDa
Excluded volume excluded_volume19743 ų
Envelope volume envelope_volume21838 ų
Hydration-shell volume shell_volume12845 ų
Envelope diameter envelope_diameter53.4
Shell Rg shell_rg20.29
Envelope Rg envelope_rg14.84
Shape Rg shape_rg14.61
Total Rg total_rg15.74
Total atoms total_atoms1114
Residues n_residues141
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 dmax52.5
Rg (real space) rg_real15.96
Rg uncertainty (real space) rg_real_error0.28
I(0) (real space) i0_real4.9080e+06
I(0) uncertainty (real space) i0_real_error5.5910e+04
Rg (reciprocal space) rg_reciprocal15.97
I(0) (reciprocal space) i0_reciprocal4908000.0000
Solution quality estimate total_estimate0.8133
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary20.6
Skewness Skewness skewness0.156
Kurtosis Kurtosis kurtosis-0.385
Angular range angular_range— – 0.4950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha751900.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.858; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)