6mcq

L. pneumophila effector kinase LegK7 in complex with human MOB1A

Method: X-RAY DIFFRACTION Dmax: 132.5 Å Quality: GOOD

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

LegK7

Legionella pneumophila subsp. pneumophila

UniProt Q5ZU83

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 11–530 Fragment:UNP residues 11-530 MOB kinase activator 1A × 1 (Q9H8S9) PEG DI(HYDROXYETHYL)ETHER × 10 P6G HEXAETHYLENE GLYCOL × 3 PG4 TETRAETHYLENE GLYCOL × 3 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;288 K;0.1 M HEPES, pH 7.5, 23% PEG600, 0.1 M lithium chloride, 20 mM succinate, pH 7.0 Resolution 2.57 Å R-free 0.245
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 11–530 Fragment:UNP residues 11-530 MOB kinase activator 1A × 1 (Q9H8S9) PEG DI(HYDROXYETHYL)ETHER × 6 PG4 TETRAETHYLENE GLYCOL × 2 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;288 K;0.1 M HEPES, pH 7.5, 23% PEG600, 0.1 M lithium chloride, 20 mM succinate, pH 7.0 Resolution 2.57 Å R-free 0.245

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.

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

View Construct and Data Evidence
UniProt name Q5ZU83_LEGPH
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–523; UniProt 11–530 Author chain C; PDBConstruct 4–523; UniProt 11–530

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 33–216 Fragment:UNP residues 33-216 LegK7 × 1 (Q5ZU83) PEG DI(HYDROXYETHYL)ETHER × 10 P6G HEXAETHYLENE GLYCOL × 3 PG4 TETRAETHYLENE GLYCOL × 3 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;288 K;0.1 M HEPES, pH 7.5, 23% PEG600, 0.1 M lithium chloride, 20 mM succinate, pH 7.0 Resolution 2.57 Å R-free 0.245
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 33–216 Fragment:UNP residues 33-216 LegK7 × 1 (Q5ZU83) PEG DI(HYDROXYETHYL)ETHER × 6 PG4 TETRAETHYLENE GLYCOL × 2 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;288 K;0.1 M HEPES, pH 7.5, 23% PEG600, 0.1 M lithium chloride, 20 mM succinate, pH 7.0 Resolution 2.57 Å R-free 0.245

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 2
Chains and sequence ranges Author chain B; PDBConstruct 4–187; UniProt 33–216 Author chain D; PDBConstruct 4–187; UniProt 33–216

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 6mcq

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6mcq
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6mcq
Deposition date deposition_date2018-09-01
Structure title titleL. pneumophila effector kinase LegK7 in complex with human MOB1A
Keywords keywordstranslocated effector, Ser/Thr protein kinase, allosteric activation, Hippo pathway, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier37.09
Radius of gyration Rg (electron density) rg_electron36.33
Forward intensity I(0) i0371029000.00
Molecular weight molecular_weight160950.0 kDa
Excluded volume excluded_volume203180 ų
Envelope volume envelope_volume266380 ų
Hydration-shell volume shell_volume59584 ų
Envelope diameter envelope_diameter141.3
Shell Rg shell_rg43.84
Envelope Rg envelope_rg36.31
Shape Rg shape_rg36.33
Total Rg total_rg36.85
Total atoms total_atoms11350
Residues n_residues1403
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 dmax132.5
Rg (real space) rg_real36.96
Rg uncertainty (real space) rg_real_error1.21
I(0) (real space) i0_real3.7100e+08
I(0) uncertainty (real space) i0_real_error6.3980e+06
Rg (reciprocal space) rg_reciprocal37.04
I(0) (reciprocal space) i0_reciprocal371100000.0000
Solution quality estimate total_estimate0.8517
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary49.3
Skewness Skewness skewness0.265
Kurtosis Kurtosis kurtosis-0.194
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha143800000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.700; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.983

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd6mcqb1
Class classa — All alpha proteins
Fold Fold folda.29 — Bromodomain-like
Superfamily Superfamily superfamilya.29.7 — Mob1/phocein
Family Family familya.29.7.1 — Mob1/phocein
Domain ID domain_idd6mcqb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd6mcqd1
Class classa — All alpha proteins
Fold Fold folda.29 — Bromodomain-like
Superfamily Superfamily superfamilya.29.7 — Mob1/phocein
Family Family familya.29.7.1 — Mob1/phocein
Domain ID domain_idd6mcqd2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id6mcqB00
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_id6mcqD00
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)