4r14

Crystal structure of human CSN6 MPN domain

Method: X-RAY DIFFRACTION Dmax: 69.8 Å Quality: REASONABLE

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

COP9 signalosome complex subunit 6

Homo sapiens

UniProt Q7L5N1

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 38–210 Chain B; UniProt 38–210 Fragment:MPN domain, UNP residues 38-210 HG MERCURY (II) ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.7;289 K;0.1M Tris pH 7.7, 26% (w/v) PEG 4000, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.60 Å R-free 0.259

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.

28 other PDB entries and 36 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CSN6_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–173; UniProt 38–210 Author chain B; PDBConstruct 1–173; UniProt 38–210

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 4r14

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4r14
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4r14
Deposition date deposition_date2014-08-04
Structure title titleCrystal structure of human CSN6 MPN domain
Keywords keywordsMPN domain, protein-protein interaction, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.89
Radius of gyration Rg (electron density) rg_electron26.35
Forward intensity I(0) i024370500.00
Molecular weight molecular_weight36607.0 kDa
Excluded volume excluded_volume44884 ų
Envelope volume envelope_volume64978 ų
Hydration-shell volume shell_volume23062 ų
Envelope diameter envelope_diameter126.9
Shell Rg shell_rg29.36
Envelope Rg envelope_rg28.63
Shape Rg shape_rg26.46
Total Rg total_rg26.39
Total atoms total_atoms2478
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 dmax69.8
Rg (real space) rg_real24.31
Rg uncertainty (real space) rg_real_error0.12
I(0) (real space) i0_real2.3200e+07
I(0) uncertainty (real space) i0_real_error2.2940e+05
Rg (reciprocal space) rg_reciprocal26.20
I(0) (reciprocal space) i0_reciprocal24370000.0000
Solution quality estimate total_estimate0.6796
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary25.2
Skewness Skewness skewness0.399
Kurtosis Kurtosis kurtosis-0.457
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha3.4970
Highest regularization parameter α highest_alpha2331000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.003; Oscil: 0.971; Stabil: 0.978; Sysdev: 0.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)