7zx4

Clathrin N-terminal domain in complex with a HURP phospho-peptide

Method: X-RAY DIFFRACTION Dmax: 102.3 Å Quality: GOOD

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

Clathrin heavy chain 1

Homo sapiens

UniProt Q00610

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–364 Not recorded Disks large-associated protein 5 × 2 (Q15398) GOL GLYCEROL × 2 CL CHLORIDE ION × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;293 K;50 mM Tris pH 7.5, 30 % PEG 6000 Resolution 2.08 Å R-free 0.249
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–364 Not recorded Disks large-associated protein 5 × 1 (Q15398) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;293 K;50 mM Tris pH 7.5, 30 % PEG 6000 Resolution 2.08 Å R-free 0.249

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 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CLH1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–364; UniProt 1–364 Author chain B; PDBConstruct 1–364; UniProt 1–364

Disks large-associated protein 5

OrganismNot specified

UniProt Q15398

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 826–846 Chain E; UniProt 826–846 Non-standard monomer:Yes (specific site not provided by mmCIF) Clathrin heavy chain 1 × 1 (Q00610) GOL GLYCEROL × 2 CL CHLORIDE ION × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;293 K;50 mM Tris pH 7.5, 30 % PEG 6000 Resolution 2.08 Å R-free 0.249
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 826–846 Non-standard monomer:Yes (specific site not provided by mmCIF) Clathrin heavy chain 1 × 1 (Q00610) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;293 K;50 mM Tris pH 7.5, 30 % PEG 6000 Resolution 2.08 Å R-free 0.249

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DLGP5_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–21; UniProt 826–846 Author chain D; PDBConstruct 1–21; UniProt 826–846 Author chain E; PDBConstruct 1–21; UniProt 826–846

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 7zx4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7zx4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7zx4
Deposition date deposition_date2022-05-20
Structure title titleClathrin N-terminal domain in complex with a HURP phospho-peptide
Keywords keywordscomplex, phospho-regulated SLiM-based interactions, HURP, DLGAP5, ENDOCYTOSIS; ENDOCYTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.56
Radius of gyration Rg (electron density) rg_electron30.94
Forward intensity I(0) i0106541000.00
Molecular weight molecular_weight82723.0 kDa
Excluded volume excluded_volume103920 ų
Envelope volume envelope_volume133310 ų
Hydration-shell volume shell_volume36296 ų
Envelope diameter envelope_diameter102.5
Shell Rg shell_rg37.77
Envelope Rg envelope_rg30.85
Shape Rg shape_rg30.98
Total Rg total_rg31.41
Total atoms total_atoms5805
Residues n_residues738
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 dmax102.3
Rg (real space) rg_real31.64
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real1.0650e+08
I(0) uncertainty (real space) i0_real_error1.4470e+06
Rg (reciprocal space) rg_reciprocal31.61
I(0) (reciprocal space) i0_reciprocal106500000.0000
Solution quality estimate total_estimate0.8862
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary32.7
Skewness Skewness skewness0.385
Kurtosis Kurtosis kurtosis-0.518
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21060000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.877; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.907

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)