Research workbench
Crystal structure of the catalytic domain of human drp-1 kinase
Analyse Crystal structure of the catalytic domain of human drp-1 kinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZWS
- Type
- protein
- Length
- 2,224 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dap-kinase related protein 1
- UniProt
- Q9UIK4
- Pockets
- 20 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Dap-kinase related protein 1 | protein | 278 | 36% helix, 17% strand | Q9UIK4 |
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 688 | 0.77 | 0.82 | 79 | empty |
| 2 | 665 | 0.77 | 0.82 | 74 | empty |
| 3 | 855 | 0.76 | 0.79 | 70 | empty |
| 4 | 585 | 0.75 | 0.82 | 65 | empty |
| 5 | 775 | 0.75 | 0.79 | 70 | empty |
Interfaces
5 interfaces between chains.
- A–B · 1052 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 1037 Ų buried · 13 hydrogen bonds · protein-protein
- E–F · 1011 Ų buried · 12 hydrogen bonds · protein-protein
- G–H · 996 Ų buried · 10 hydrogen bonds · protein-protein
- D–F · 11 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1ZWS · Crystal structure of the catalytic domain of human DRP-1 kinase · the same entry in another collection · chain H against H, TM-score 1.00
- Q9UIK4 · AlphaFold monomer V2.0 prediction for death-associated protein kinase 2 (Q9UIK4) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q9UIK4
- Elsewhere: RCSB PDB 1ZWS · PDBe 1ZWS · UniProt Q9UIK4
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