Research workbench
Structure of dimeric phosphorylated Pediculus humanus (Ph) PINK1 with kinked alpha-C helix in chain B
Analyse Structure of dimeric phosphorylated Pediculus humanus (Ph) PINK1 with kinked… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7T4K
- Type
- protein
- Length
- 782 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.25
- Source
- Pediculus humanus corporis
- Molecule
- Serine/threonine-protein kinase PINK1, putative
- EC
- 2.7.11.1
- UniProt
- E0W1I1
- Pockets
- 10 · best druggability 0.78
Structure
electron microscopy · resolution 3.25 · 2 distinct chains · 37% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serine/threonine-protein kinase PINK1, putative (EC 2.7.11.1) | protein | 379 | 38% helix, 16% strand | E0W1I1 |
| B | Serine/threonine-protein kinase PINK1, putative (EC 2.7.11.1) | protein | 403 | 37% helix, 15% strand | E0W1I1 |
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 468 | 0.78 | 0.86 | 66 | empty |
| 2 | 128 | 0.62 | 0.86 | 26 | empty |
| 3 | 113 | 0.62 | 0.87 | 23 | empty |
| 4 | 120 | 0.60 | 0.86 | 27 | empty |
| 5 | 88 | 0.41 | 0.78 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1470 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 7T4K · Structure of dimeric phosphorylated pediculus humanus (pH) PINK1 with kinked alpha-C… · the same entry in another collection · chain A against A, TM-score 1.00
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 E0W1I1
- Elsewhere: RCSB PDB 7T4K · PDBe 7T4K · UniProt E0W1I1
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