Research workbench
L. pneumophila effector kinase LEGK7 in complex with human MOB1A
Analyse L. pneumophila effector kinase LEGK7 in complex with human MOB1A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MCQ
- Type
- protein
- Length
- 1,403 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- LEGK7; Mob kinase activator 1A
- EC
- 2.7.11.1
- UniProt
- Q5ZU83, Q9H8S9
- Ligands
- ZN
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 4 distinct chains · 53% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | LEGK7 (EC 2.7.11.1) | protein | 519 | 52% helix, 9% strand | Q5ZU83 |
| B | Mob kinase activator 1A | protein | 183 | 55% helix, 2% strand | Q9H8S9 |
| C | LEGK7 (EC 2.7.11.1) | protein | 519 | 53% helix, 9% strand | Q5ZU83 |
| D | Mob kinase activator 1A | protein | 182 | 54% helix, 2% strand | Q9H8S9 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains B, D
- PEG · Di(hydroxyethyl)ether · additive · 16 copies · chains A, B, C, D
- PG4 · Tetraethylene glycol · additive · 5 copies · chains A, B, C, D
- P6G · Hexaethylene glycol · additive · 3 copies · chains A, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 934 | 0.82 | 0.83 | 66 | empty |
| 2 | 622 | 0.79 | 0.85 | 64 | PEG |
| 3 | 672 | 0.78 | 0.83 | 69 | P6G |
| 4 | 665 | 0.77 | 0.82 | 76 | PEG |
| 5 | 117 | 0.77 | 0.96 | 25 | empty |
Interfaces
3 interfaces between chains.
- C–D · 1638 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 1573 Ų buried · 26 hydrogen bonds · protein-protein
- A–C · 1211 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q5ZU83
- Every structure of UniProt Q9H8S9
- Elsewhere: RCSB PDB 6MCQ · PDBe 6MCQ · UniProt Q5ZU83 · UniProt Q9H8S9
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