4dra

Crystal structure of MHF complex

Method: X-RAY DIFFRACTION Dmax: 105.8 Å Quality: GOOD

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

Centromere protein S

Homo sapiens

UniProt Q8N2Z9

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 1–107 Chain D; UniProt 1–107 Fragment:C-terminus deleted, UNP residues 1-107 Centromere protein X × 2 (A8MT69) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;285 K;0.1M HEPES-NaOH, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 285K Resolution 2.41 Å R-free 0.242
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–107 Chain C; UniProt 1–107 Fragment:C-terminus deleted, UNP residues 1-107 Centromere protein X × 2 (A8MT69) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;285 K;0.1M HEPES-NaOH, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 285K Resolution 2.41 Å R-free 0.242

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.

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

View Construct and Data Evidence
UniProt name CENPS_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 7–113; UniProt 1–107 Author chain B; PDBConstruct 7–113; UniProt 1–107 Author chain C; PDBConstruct 7–113; UniProt 1–107 Author chain D; PDBConstruct 7–113; UniProt 1–107

Centromere protein X

Homo sapiens

UniProt A8MT69

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 E; UniProt 1–81 Chain H; UniProt 1–81 Not recorded Centromere protein S × 2 (Q8N2Z9) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;285 K;0.1M HEPES-NaOH, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 285K Resolution 2.41 Å R-free 0.242
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain F; UniProt 1–81 Chain G; UniProt 1–81 Not recorded Centromere protein S × 2 (Q8N2Z9) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;285 K;0.1M HEPES-NaOH, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 285K Resolution 2.41 Å R-free 0.242

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.

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

View Construct and Data Evidence
UniProt name CENPX_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 4–84; UniProt 1–81 Author chain F; PDBConstruct 4–84; UniProt 1–81 Author chain G; PDBConstruct 4–84; UniProt 1–81 Author chain H; PDBConstruct 4–84; UniProt 1–81

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 4dra

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4dra
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4dra
Deposition date deposition_date2012-02-17
Structure title titleCrystal structure of MHF complex
Keywords keywordsDNA binding complex, DNA damage repair, Histone-fold, 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_guinier32.03
Radius of gyration Rg (electron density) rg_electron31.31
Forward intensity I(0) i086980100.00
Molecular weight molecular_weight74322.0 kDa
Excluded volume excluded_volume93542 ų
Envelope volume envelope_volume124110 ų
Hydration-shell volume shell_volume34172 ų
Envelope diameter envelope_diameter111.9
Shell Rg shell_rg36.92
Envelope Rg envelope_rg30.95
Shape Rg shape_rg31.31
Total Rg total_rg31.85
Total atoms total_atoms5227
Residues n_residues677
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 dmax105.8
Rg (real space) rg_real32.09
Rg uncertainty (real space) rg_real_error0.95
I(0) (real space) i0_real8.6980e+07
I(0) uncertainty (real space) i0_real_error1.4780e+06
Rg (reciprocal space) rg_reciprocal32.07
I(0) (reciprocal space) i0_reciprocal86980000.0000
Solution quality estimate total_estimate0.8930
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.362
Kurtosis Kurtosis kurtosis-0.387
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10880000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.901; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.976; Smooth: 0.927

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

Domain ID domain_id4draA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4draB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4draC00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4draD00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4draE01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily4980
Domain ID domain_id4draE02
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology130 — GTP Cyclohydrolase I; Chain A, domain 1
Homologous superfamily homologous superfamily30
Domain ID domain_id4draF01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily4980
Domain ID domain_id4draF02
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology130 — GTP Cyclohydrolase I; Chain A, domain 1
Homologous superfamily homologous superfamily30
Domain ID domain_id4draG01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily4980
Domain ID domain_id4draG02
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology130 — GTP Cyclohydrolase I; Chain A, domain 1
Homologous superfamily homologous superfamily30
Domain ID domain_id4draH01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily4980
Domain ID domain_id4draH02
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology130 — GTP Cyclohydrolase I; Chain A, domain 1
Homologous superfamily homologous superfamily30

8. Citations (1)

9. Files and Curves (10)