7eaa

crystal structure of NDP52 SKICH domain in complex with RB1CC1 coiled-coil domain

Method: X-RAY DIFFRACTION Dmax: 161.2 Å Quality: REASONABLE

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

RB1-inducible coiled-coil protein 1

Homo sapiens

UniProt Q8TDY2

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1286–1395 Chain D; UniProt 1286–1395 Not recorded Calcium-binding and coiled-coil domain-containing protein 2 × 2 (Q13137) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;0.1 M MgCl2, 0.1 M MES pH 6.0, 8% PEG6000 Resolution 2.60 Å R-free 0.253

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.

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

View Construct and Data Evidence
UniProt name RBCC1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 5–114; UniProt 1286–1395 Author chain D; PDBConstruct 5–114; UniProt 1286–1395

Calcium-binding and coiled-coil domain-containing protein 2

Homo sapiens

UniProt Q13137

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 10–141 Chain B; UniProt 10–141 Not recorded RB1-inducible coiled-coil protein 1 × 2 (Q8TDY2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;0.1 M MgCl2, 0.1 M MES pH 6.0, 8% PEG6000 Resolution 2.60 Å R-free 0.253

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.

9 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CACO2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 5–136; UniProt 10–141 Author chain B; PDBConstruct 5–136; UniProt 10–141

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 7eaa

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7eaa
Deposition date deposition_date2021-03-06
Structure title titlecrystal structure of NDP52 SKICH domain in complex with RB1CC1 coiled-coil domain
Keywords keywordsNDP52 SKICH, complex, RB1CC1 coiled-coil, 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_guinier41.19
Radius of gyration Rg (electron density) rg_electron42.84
Forward intensity I(0) i043695800.00
Molecular weight molecular_weight52339.0 kDa
Excluded volume excluded_volume65409 ų
Envelope volume envelope_volume91950 ų
Hydration-shell volume shell_volume22396 ų
Envelope diameter envelope_diameter165.7
Shell Rg shell_rg37.91
Envelope Rg envelope_rg43.02
Shape Rg shape_rg42.78
Total Rg total_rg42.68
Total atoms total_atoms3690
Residues n_residues441
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 dmax161.2
Rg (real space) rg_real42.42
Rg uncertainty (real space) rg_real_error2.82
I(0) (real space) i0_real4.3700e+07
I(0) uncertainty (real space) i0_real_error9.0460e+05
Rg (reciprocal space) rg_reciprocal41.20
I(0) (reciprocal space) i0_reciprocal43640000.0000
Solution quality estimate total_estimate0.6226
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.4
Skewness Skewness skewness0.845
Kurtosis Kurtosis kurtosis-0.201
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2369000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.055; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.015; Smooth: 0.909

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)