4geh

Crystal structure of MST4 dimerization domain complex with PDCD10

Method: X-RAY DIFFRACTION Dmax: 100.8 Å Quality: GOOD

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

Programmed cell death protein 10

Homo sapiens

UniProt Q9BUL8

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 9–212 Fragment:UNP residues 9-212 Serine/threonine-protein kinase MST4 × 1 (Q9P289) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;2% v/v Tacsimate pH 6.0, 0.1M BIS-TRIS pH 6.5, 18% w/v PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 1.95 Å R-free 0.253
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 9–212 Fragment:UNP residues 9-212 Serine/threonine-protein kinase MST4 × 1 (Q9P289) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;2% v/v Tacsimate pH 6.0, 0.1M BIS-TRIS pH 6.5, 18% w/v PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 1.95 Å R-free 0.253

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.

9 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PDC10_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–207; UniProt 9–212 Author chain C; PDBConstruct 4–207; UniProt 9–212

Serine/threonine-protein kinase MST4

Homo sapiens

UniProt Q9P289

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 B; UniProt 325–413 Fragment:Dimerization domain, UNP residues 325-413 Programmed cell death protein 10 × 1 (Q9BUL8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;2% v/v Tacsimate pH 6.0, 0.1M BIS-TRIS pH 6.5, 18% w/v PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 1.95 Å R-free 0.253
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 325–413 Fragment:Dimerization domain, UNP residues 325-413 Programmed cell death protein 10 × 1 (Q9BUL8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;2% v/v Tacsimate pH 6.0, 0.1M BIS-TRIS pH 6.5, 18% w/v PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 1.95 Å R-free 0.253

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.

8 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MST4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–91; UniProt 325–413 Author chain D; PDBConstruct 3–91; UniProt 325–413

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 4geh

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4geh
Deposition date deposition_date2012-08-02
Structure title titleCrystal structure of MST4 dimerization domain complex with PDCD10
Keywords keywords;alpha helix-rich protein, serine/threonine-protein kinase, protein binding, cell proliferation, cell growth, PROTEIN BINDING-TRANSFERASE complex ;; PROTEIN BINDING/TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.36
Radius of gyration Rg (electron density) rg_electron30.02
Forward intensity I(0) i055822400.00
Molecular weight molecular_weight60008.0 kDa
Excluded volume excluded_volume75897 ų
Envelope volume envelope_volume98205 ų
Hydration-shell volume shell_volume28767 ų
Envelope diameter envelope_diameter105.1
Shell Rg shell_rg35.18
Envelope Rg envelope_rg29.70
Shape Rg shape_rg30.05
Total Rg total_rg30.44
Total atoms total_atoms4213
Residues n_residues530
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 dmax100.8
Rg (real space) rg_real30.45
Rg uncertainty (real space) rg_real_error1.02
I(0) (real space) i0_real5.5820e+07
I(0) uncertainty (real space) i0_real_error8.8750e+05
Rg (reciprocal space) rg_reciprocal30.42
I(0) (reciprocal space) i0_reciprocal55820000.0000
Solution quality estimate total_estimate0.8142
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.0
Skewness Skewness skewness0.377
Kurtosis Kurtosis kurtosis-0.446
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8500000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.890; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.913; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id4gehA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily1950
Domain ID domain_id4gehB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology12 — Lyase 2-enoyl-coa Hydratase; Chain A, domain 2
Homologous superfamily homologous superfamily70
Domain ID domain_id4gehC00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily1950
Domain ID domain_id4gehD00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology12 — Lyase 2-enoyl-coa Hydratase; Chain A, domain 2
Homologous superfamily homologous superfamily70

8. Citations (1)

9. Files and Curves (10)