4j1v

Functional and structural studies of MOBKL1B, a Salvador/Warts/Hippo tumor suppressor pathway, in HCV replication

Method: X-RAY DIFFRACTION Dmax: 90.3 Å Quality: GOOD

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

MOB kinase activator 1A

Homo sapiens

UniProt Q9H8S9

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 33–216 Not recorded NS5A domain II peptide × 2 (Q99IB8) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;279 K;0.1 M HEPES, 0.1 M KCl, 15% PEG5000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K Resolution 1.95 Å R-free 0.225
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 33–216 Not recorded NS5A domain II peptide × 2 (Q99IB8) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;279 K;0.1 M HEPES, 0.1 M KCl, 15% PEG5000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K Resolution 1.95 Å R-free 0.225

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.

10 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MOB1A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–184; UniProt 33–216 Author chain C; PDBConstruct 1–184; UniProt 33–216

NS5A domain II peptide

OrganismNot specified

UniProt Q99IB8

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 E; UniProt 2284–2303 Chain G; UniProt 2284–2303 Not recorded MOB kinase activator 1A × 1 (Q9H8S9) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;279 K;0.1 M HEPES, 0.1 M KCl, 15% PEG5000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K Resolution 1.95 Å R-free 0.225
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 2284–2303 Chain H; UniProt 2284–2303 Not recorded MOB kinase activator 1A × 1 (Q9H8S9) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;279 K;0.1 M HEPES, 0.1 M KCl, 15% PEG5000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K Resolution 1.95 Å R-free 0.225

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.

31 other PDB entries and 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POLG_HCVJF
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–20; UniProt 2284–2303 Author chain F; PDBConstruct 1–20; UniProt 2284–2303 Author chain G; PDBConstruct 1–20; UniProt 2284–2303 Author chain H; PDBConstruct 1–20; UniProt 2284–2303

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 4j1v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4j1v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4j1v
Deposition date deposition_date2013-02-02
Structure title titleFunctional and structural studies of MOBKL1B, a Salvador/Warts/Hippo tumor suppressor pathway, in HCV replication
Keywords keywordsHCV NS5A binding protein, NS5A, PEPTIDE BINDING PROTEIN-VIRAL PROTEIN complex; PEPTIDE BINDING PROTEIN/VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.93
Radius of gyration Rg (electron density) rg_electron28.25
Forward intensity I(0) i030566500.00
Molecular weight molecular_weight44510.0 kDa
Excluded volume excluded_volume56231 ų
Envelope volume envelope_volume72864 ų
Hydration-shell volume shell_volume22445 ų
Envelope diameter envelope_diameter95.9
Shell Rg shell_rg34.26
Envelope Rg envelope_rg27.76
Shape Rg shape_rg28.23
Total Rg total_rg28.99
Total atoms total_atoms3140
Residues n_residues380
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 dmax90.3
Rg (real space) rg_real29.07
Rg uncertainty (real space) rg_real_error0.85
I(0) (real space) i0_real3.0570e+07
I(0) uncertainty (real space) i0_real_error5.2230e+05
Rg (reciprocal space) rg_reciprocal29.01
I(0) (reciprocal space) i0_reciprocal30570000.0000
Solution quality estimate total_estimate0.8591
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.6
Skewness Skewness skewness0.345
Kurtosis Kurtosis kurtosis-0.762
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5618000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.871; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.746; Smooth: 0.805

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id4j1vA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily30 — MOB kinase activator
Domain ID domain_id4j1vC00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily30 — MOB kinase activator

8. Citations (1)

9. Files and Curves (10)