7pb4

Cenp-HIK 3-protein complex

Method: X-RAY DIFFRACTION Dmax: 79.4 Å Quality: GOOD

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

Centromere protein H

Homo sapiens

UniProt Q9H3R5

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 H; UniProt 199–247 Not recorded Centromere protein I × 1 (Q92674) Centromere protein K × 1 (Q9BS16) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;10% PEG 8k, 100 mM imidazole pH 8 Resolution 2.49 Å R-free 0.283

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.

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

View Construct and Data Evidence
UniProt name CENPH_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain H; PDBConstruct 1–49; UniProt 199–247

Centromere protein I

Homo sapiens

UniProt Q92674

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 I; UniProt 64–281 Not recorded Centromere protein H × 1 (Q9H3R5) Centromere protein K × 1 (Q9BS16) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;10% PEG 8k, 100 mM imidazole pH 8 Resolution 2.49 Å R-free 0.283

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.

11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CENPI_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain I; PDBConstruct 2–219; UniProt 64–281

Centromere protein K

Homo sapiens

UniProt Q9BS16

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 K; UniProt 165–269 Not recorded Centromere protein H × 1 (Q9H3R5) Centromere protein I × 1 (Q92674) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;10% PEG 8k, 100 mM imidazole pH 8 Resolution 2.49 Å R-free 0.283

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.

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

View Construct and Data Evidence
UniProt name CENPK_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain K; PDBConstruct 1–105; UniProt 165–269

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 7pb4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7pb4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7pb4
Deposition date deposition_date2021-07-30
Structure title titleCenp-HIK 3-protein complex
Keywords keywordsinner kinetochore, 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_guinier23.90
Radius of gyration Rg (electron density) rg_electron22.80
Forward intensity I(0) i024825400.00
Molecular weight molecular_weight40651.0 kDa
Excluded volume excluded_volume52080 ų
Envelope volume envelope_volume62745 ų
Hydration-shell volume shell_volume23457 ų
Envelope diameter envelope_diameter82.0
Shell Rg shell_rg29.37
Envelope Rg envelope_rg23.13
Shape Rg shape_rg22.75
Total Rg total_rg23.84
Total atoms total_atoms2864
Residues n_residues353
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 dmax79.4
Rg (real space) rg_real23.90
Rg uncertainty (real space) rg_real_error0.69
I(0) (real space) i0_real2.4830e+07
I(0) uncertainty (real space) i0_real_error3.4130e+05
Rg (reciprocal space) rg_reciprocal23.90
I(0) (reciprocal space) i0_reciprocal24830000.0000
Solution quality estimate total_estimate0.7783
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary26.1
Skewness Skewness skewness0.368
Kurtosis Kurtosis kurtosis-0.340
Angular range angular_range— – 0.3300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6180000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.745; Stabil: 0.967; Sysdev: 1.000; Positv: 1.000; Valcen: 0.978; 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)