3nqj

Crystal structure of (CENP-A/H4)2 heterotetramer

Method: X-RAY DIFFRACTION Dmax: 56.8 Å Quality: GOOD

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

Histone H3-like centromeric protein A

Homo sapiens

UniProt P49450

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 60–140 Fragment:UNP residues 60-140 Histone H4 × 2 (P62805) PO4 PHOSPHATE ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;295 K;0.17 M ammonium sulfate, 0.085 M sodium cacodylate (pH 6.5), 25.5% PEG-8000, 15% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.10 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.

33 other PDB entries and 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CENPA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–82; UniProt 60–140

Histone H4

Homo Sapiens

UniProt P62805

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 B; UniProt 21–103 Fragment:UNP residues 21-103 Histone H3-like centromeric protein A × 2 (P49450) PO4 PHOSPHATE ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;295 K;0.17 M ammonium sulfate, 0.085 M sodium cacodylate (pH 6.5), 25.5% PEG-8000, 15% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.10 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.

581 other PDB entries and 633 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–84; UniProt 21–103

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 3nqj

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3nqj
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3nqj
Deposition date deposition_date2010-06-29
Structure title titleCrystal structure of (CENP-A/H4)2 heterotetramer
Keywords keywordsalpha helix, histone fold, centromere, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.41
Radius of gyration Rg (electron density) rg_electron16.26
Forward intensity I(0) i05404570.00
Molecular weight molecular_weight16815.0 kDa
Excluded volume excluded_volume21173 ų
Envelope volume envelope_volume24517 ų
Hydration-shell volume shell_volume13281 ų
Envelope diameter envelope_diameter57.8
Shell Rg shell_rg21.39
Envelope Rg envelope_rg16.48
Shape Rg shape_rg16.22
Total Rg total_rg17.30
Total atoms total_atoms1182
Residues n_residues145
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 dmax56.8
Rg (real space) rg_real17.40
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real5.4050e+06
I(0) uncertainty (real space) i0_real_error6.6700e+04
Rg (reciprocal space) rg_reciprocal17.40
I(0) (reciprocal space) i0_reciprocal5405000.0000
Solution quality estimate total_estimate0.8079
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.9
Skewness Skewness skewness0.315
Kurtosis Kurtosis kurtosis-0.334
Angular range angular_range— – 0.4550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1020000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.839; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3nqja_
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.1 — Nucleosome core histones
Domain ID domain_idd3nqjb_
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.1 — Nucleosome core histones

CATH v4.4 (2 domains)

Domain ID domain_id3nqjA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id3nqjB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A

8. Citations (1)

9. Files and Curves (10)