7sfy

Crystal structure of human Mis18ab_cc

Method: X-RAY DIFFRACTION Dmax: 69.2 Å Quality: REASONABLE

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

Protein Mis18-alpha

Homo sapiens

UniProt Q9NYP9

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 191–233 Chain B; UniProt 191–233 Not recorded Protein Mis18-beta × 1 (O43482) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;295.15 K;Magnesium acetate, PEG 3350 Resolution 2.50 Å R-free 0.280
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 191–233 Chain E; UniProt 191–233 Not recorded Protein Mis18-beta × 1 (O43482) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;295.15 K;Magnesium acetate, PEG 3350 Resolution 2.50 Å R-free 0.280

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.

2 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MS18A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–46; UniProt 191–233 Author chain B; PDBConstruct 4–46; UniProt 191–233 Author chain D; PDBConstruct 4–46; UniProt 191–233 Author chain E; PDBConstruct 4–46; UniProt 191–233

Protein Mis18-beta

Homo sapiens

UniProt O43482

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 188–229 Not recorded Protein Mis18-alpha × 2 (Q9NYP9) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;295.15 K;Magnesium acetate, PEG 3350 Resolution 2.50 Å R-free 0.280
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 188–229 Not recorded Protein Mis18-alpha × 2 (Q9NYP9) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;295.15 K;Magnesium acetate, PEG 3350 Resolution 2.50 Å R-free 0.280

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name MS18B_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–42; UniProt 188–229 Author chain F; PDBConstruct 1–42; UniProt 188–229

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 7sfy

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7sfy
Deposition date deposition_date2021-10-04
Structure title titleCrystal structure of human Mis18ab_cc
Keywords keywordsMis18ab complex, 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_guinier20.52
Radius of gyration Rg (electron density) rg_electron19.53
Forward intensity I(0) i09097850.00
Molecular weight molecular_weight23295.0 kDa
Excluded volume excluded_volume29774 ų
Envelope volume envelope_volume36390 ų
Hydration-shell volume shell_volume16323 ų
Envelope diameter envelope_diameter69.1
Shell Rg shell_rg24.85
Envelope Rg envelope_rg19.83
Shape Rg shape_rg19.53
Total Rg total_rg20.42
Total atoms total_atoms1627
Residues n_residues202
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 dmax69.2
Rg (real space) rg_real20.49
Rg uncertainty (real space) rg_real_error0.57
I(0) (real space) i0_real9.0980e+06
I(0) uncertainty (real space) i0_real_error1.2610e+05
Rg (reciprocal space) rg_reciprocal20.49
I(0) (reciprocal space) i0_reciprocal9098000.0000
Solution quality estimate total_estimate0.6562
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks4
Primary peak position r_peak_primary28.1
Skewness Skewness skewness0.235
Kurtosis Kurtosis kurtosis-0.450
Angular range angular_range— – 0.3850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3732000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.803; Stabil: 0.999; Sysdev: 0.387; Positv: 1.000; Valcen: 0.958; 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)