6b5q

DCN1 bound to 38

Method: X-RAY DIFFRACTION Dmax: 78.3 Å Quality: GOOD

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

DCN1-like protein 1

Homo sapiens

UniProt Q96GG9

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 58–259 Not recorded Peptidomimetic Inhibitors DI-591 × 1 PGE TRIETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;37 % PEG 300, 0.1 M phosphate-citrate pH 4.2 Resolution 2.16 Å R-free 0.241
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 58–259 Not recorded Peptidomimetic Inhibitors DI-591 × 1 PGE TRIETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;37 % PEG 300, 0.1 M phosphate-citrate pH 4.2 Resolution 2.16 Å R-free 0.241

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.

20 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DCNL1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 24–225; UniProt 58–259 Author chain B; PDBConstruct 24–225; UniProt 58–259

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 6b5q

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6b5q
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6b5q
Deposition date deposition_date2017-09-29
Structure title titleDCN1 bound to 38
Keywords keywordsE3 ligase, complex, Ligase-Inhibitor complex, LIGASE; Ligase/Inhibitor
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.09
Radius of gyration Rg (electron density) rg_electron22.01
Forward intensity I(0) i030771700.00
Molecular weight molecular_weight44432.0 kDa
Excluded volume excluded_volume56298 ų
Envelope volume envelope_volume65829 ų
Hydration-shell volume shell_volume25014 ų
Envelope diameter envelope_diameter78.8
Shell Rg shell_rg28.88
Envelope Rg envelope_rg22.12
Shape Rg shape_rg22.00
Total Rg total_rg22.90
Total atoms total_atoms3226
Residues n_residues376
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 dmax78.3
Rg (real space) rg_real23.02
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real3.0770e+07
I(0) uncertainty (real space) i0_real_error4.7550e+05
Rg (reciprocal space) rg_reciprocal23.04
I(0) (reciprocal space) i0_reciprocal30770000.0000
Solution quality estimate total_estimate0.8762
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.7
Skewness Skewness skewness0.287
Kurtosis Kurtosis kurtosis-0.289
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13690000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.797; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id6b5qA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id6b5qB01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand

8. Citations (1)

9. Files and Curves (10)