5jja

Crystal structure of a PP2A B56gamma/BubR1 complex

Method: X-RAY DIFFRACTION Dmax: 126.4 Å Quality: GOOD

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

Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform

Homo sapiens

UniProt Q13362

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 30–380 Not recorded Mitotic checkpoint serine/threonine-protein kinase BUB1 beta × 1 (O60566) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.1 M HEPES pH 7.5 and 20% PEG 3350 Resolution 2.35 Å R-free 0.204
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 30–380 Not recorded Mitotic checkpoint serine/threonine-protein kinase BUB1 beta × 1 (O60566) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.1 M HEPES pH 7.5 and 20% PEG 3350 Resolution 2.35 Å R-free 0.204

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.

20 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name 2A5G_HUMAN
Isoform Q13362-3
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–352; UniProt 30–380 Author chain B; PDBConstruct 2–352; UniProt 30–380

Mitotic checkpoint serine/threonine-protein kinase BUB1 beta

Homo sapiens

UniProt O60566

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 661–734 Mutation:S670D, S676D, T680D Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform × 1 (Q13362) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.1 M HEPES pH 7.5 and 20% PEG 3350 Resolution 2.35 Å R-free 0.204
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 661–734 Mutation:S670D, S676D, T680D Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform × 1 (Q13362) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.1 M HEPES pH 7.5 and 20% PEG 3350 Resolution 2.35 Å R-free 0.204

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.

6 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BUB1B_HUMAN
Isoform O60566-3
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 2–75; UniProt 661–734 Author chain D; PDBConstruct 2–75; UniProt 661–734

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 5jja

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5jja
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5jja
Deposition date deposition_date2016-04-22
Structure title titleCrystal structure of a PP2A B56gamma/BubR1 complex
Keywords keywordsPP2A, BubR1, B56gamma, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier37.73
Radius of gyration Rg (electron density) rg_electron37.58
Forward intensity I(0) i084340100.00
Molecular weight molecular_weight80408.0 kDa
Excluded volume excluded_volume103310 ų
Envelope volume envelope_volume136800 ų
Hydration-shell volume shell_volume32303 ų
Envelope diameter envelope_diameter127.5
Shell Rg shell_rg40.55
Envelope Rg envelope_rg37.35
Shape Rg shape_rg37.58
Total Rg total_rg37.82
Total atoms total_atoms5687
Residues n_residues682
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 dmax126.4
Rg (real space) rg_real38.02
Rg uncertainty (real space) rg_real_error1.57
I(0) (real space) i0_real8.4340e+07
I(0) uncertainty (real space) i0_real_error1.5720e+06
Rg (reciprocal space) rg_reciprocal37.85
I(0) (reciprocal space) i0_reciprocal84330000.0000
Solution quality estimate total_estimate0.8299
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.1
Skewness Skewness skewness0.355
Kurtosis Kurtosis kurtosis-0.736
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10640000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.780; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.715; Smooth: 0.737

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd5jjaa1
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.1 — ARM repeat
Family Family familya.118.1.20 — B56-like
Domain ID domain_idd5jjaa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd5jjab_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.1 — ARM repeat
Family Family familya.118.1.20 — B56-like

CATH v4.4 (2 domains)

Domain ID domain_id5jjaA00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant
Domain ID domain_id5jjaB00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant

8. Citations (1)

9. Files and Curves (10)