4ne5

Human MHF1-MHF2 complex

Method: X-RAY DIFFRACTION Dmax: 102.9 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 14–105 Chain E; UniProt 14–105 Non-standard monomer:Yes (specific site not provided by mmCIF) Centromere protein X × 2 (A8MT69) X-RAY DIFFRACTION X-ray crystallization conditions:Micro-batch under oil;300 K;Micro-batch under oil, temperature 300K Resolution 2.50 Å R-free 0.264
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 14–105 Chain G; UniProt 14–105 Non-standard monomer:Yes (specific site not provided by mmCIF) Centromere protein X × 2 (A8MT69) X-RAY DIFFRACTION X-ray crystallization conditions:Micro-batch under oil;300 K;Micro-batch under oil, temperature 300K Resolution 2.50 Å R-free 0.264

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 1–92; UniProt 14–105 Author chain C; PDBConstruct 1–92; UniProt 14–105 Author chain E; PDBConstruct 1–92; UniProt 14–105 Author chain G; PDBConstruct 1–92; UniProt 14–105

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 B; UniProt 8–81 Chain F; UniProt 8–81 Non-standard monomer:Yes (specific site not provided by mmCIF) Centromere protein S × 2 (Q8N2Z9) X-RAY DIFFRACTION X-ray crystallization conditions:Micro-batch under oil;300 K;Micro-batch under oil, temperature 300K Resolution 2.50 Å R-free 0.264
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 8–81 Chain H; UniProt 8–81 Non-standard monomer:Yes (specific site not provided by mmCIF) Centromere protein S × 2 (Q8N2Z9) X-RAY DIFFRACTION X-ray crystallization conditions:Micro-batch under oil;300 K;Micro-batch under oil, temperature 300K Resolution 2.50 Å R-free 0.264

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 B; PDBConstruct 1–74; UniProt 8–81 Author chain D; PDBConstruct 1–74; UniProt 8–81 Author chain F; PDBConstruct 1–74; UniProt 8–81 Author chain H; PDBConstruct 1–74; UniProt 8–81

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 4ne5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4ne5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4ne5
Deposition date deposition_date2013-10-28
Structure title titleHuman MHF1-MHF2 complex
Keywords keywordsHistone fold, DNA repair, genome maintenance, Fanconi Anemia, FancM, Nucleus, 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_guinier31.89
Radius of gyration Rg (electron density) rg_electron31.29
Forward intensity I(0) i093844900.00
Molecular weight molecular_weight76507.0 kDa
Excluded volume excluded_volume95899 ų
Envelope volume envelope_volume125880 ų
Hydration-shell volume shell_volume34701 ų
Envelope diameter envelope_diameter109.1
Shell Rg shell_rg36.90
Envelope Rg envelope_rg30.92
Shape Rg shape_rg31.28
Total Rg total_rg31.85
Total atoms total_atoms5332
Residues n_residues656
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 dmax102.9
Rg (real space) rg_real31.96
Rg uncertainty (real space) rg_real_error0.84
I(0) (real space) i0_real9.3840e+07
I(0) uncertainty (real space) i0_real_error1.5360e+06
Rg (reciprocal space) rg_reciprocal31.93
I(0) (reciprocal space) i0_reciprocal93840000.0000
Solution quality estimate total_estimate0.8940
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.0
Skewness Skewness skewness0.367
Kurtosis Kurtosis kurtosis-0.385
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11660000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.926; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.850

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_id4ne5A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4ne5B01
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_id4ne5B02
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology130 — GTP Cyclohydrolase I; Chain A, domain 1
Homologous superfamily homologous superfamily30
Domain ID domain_id4ne5C00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4ne5D01
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_id4ne5D02
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology130 — GTP Cyclohydrolase I; Chain A, domain 1
Homologous superfamily homologous superfamily30
Domain ID domain_id4ne5E00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4ne5F01
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_id4ne5F02
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology130 — GTP Cyclohydrolase I; Chain A, domain 1
Homologous superfamily homologous superfamily30
Domain ID domain_id4ne5G00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4ne5H01
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_id4ne5H02
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)