7sfz

Crystal structure of Mis18a-yippee domain

Method: X-RAY DIFFRACTION Dmax: 113.5 Å Quality: GOOD

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 77–190 Chain B; UniProt 77–190 Not recorded ZN ZINC ION × 2 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;295.15 K;Ammonium sulfate, PEG 400, HEPES Resolution 3.00 Å R-free 0.250
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 77–190 Chain D; UniProt 77–190 Not recorded ZN ZINC ION × 2 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;295.15 K;Ammonium sulfate, PEG 400, HEPES Resolution 3.00 Å R-free 0.250
3 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 77–190 Chain F; UniProt 77–190 Not recorded ZN ZINC ION × 2 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;295.15 K;Ammonium sulfate, PEG 400, HEPES Resolution 3.00 Å R-free 0.250
4 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 77–190 Chain H; UniProt 77–190 Not recorded ZN ZINC ION × 2 SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;295.15 K;Ammonium sulfate, PEG 400, HEPES Resolution 3.00 Å R-free 0.250

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 3 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 1–114; UniProt 77–190 Author chain B; PDBConstruct 1–114; UniProt 77–190 Author chain C; PDBConstruct 1–114; UniProt 77–190 Author chain D; PDBConstruct 1–114; UniProt 77–190 Author chain E; PDBConstruct 1–114; UniProt 77–190 Author chain F; PDBConstruct 1–114; UniProt 77–190 Author chain G; PDBConstruct 1–114; UniProt 77–190 Author chain H; PDBConstruct 1–114; UniProt 77–190

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 7sfz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7sfz
Deposition date deposition_date2021-10-04
Structure title titleCrystal structure of Mis18a-yippee domain
Keywords keywordsMis18a, 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_guinier34.36
Radius of gyration Rg (electron density) rg_electron34.14
Forward intensity I(0) i0121045000.00
Molecular weight molecular_weight84004.0 kDa
Excluded volume excluded_volume103560 ų
Envelope volume envelope_volume149040 ų
Hydration-shell volume shell_volume35982 ų
Envelope diameter envelope_diameter127.2
Shell Rg shell_rg41.38
Envelope Rg envelope_rg33.46
Shape Rg shape_rg34.24
Total Rg total_rg34.41
Total atoms total_atoms5780
Residues n_residues748
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 dmax113.5
Rg (real space) rg_real34.33
Rg uncertainty (real space) rg_real_error0.98
I(0) (real space) i0_real1.2100e+08
I(0) uncertainty (real space) i0_real_error1.9410e+06
Rg (reciprocal space) rg_reciprocal34.35
I(0) (reciprocal space) i0_reciprocal121000000.0000
Solution quality estimate total_estimate0.8980
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.5
Skewness Skewness skewness0.231
Kurtosis Kurtosis kurtosis-0.472
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6658000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.919; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.916

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)