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Crystal structure of the ISHP608 transposase
Analyse Crystal structure of the ISHP608 transposase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2A6M
- Type
- protein
- Length
- 280 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ISHP608 transposase
- UniProt
- Q933Z0
- Pockets
- 4 · best druggability 0.48
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ISHP608 transposase | protein | 130 | 41% helix, 30% strand | Q933Z0 |
| B | ISHP608 transposase | protein | 150 | 38% helix, 22% strand | Q933Z0 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 165 | 0.48 | 0.77 | 24 | empty |
| 2 | 167 | 0.44 | 0.75 | 27 | empty |
| 3 | 52 | 0.35 | 0.79 | 19 | empty |
| 4 | 61 | 0.29 | 0.74 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1842 Ų buried · 33 hydrogen bonds · protein-protein
Compared structures
- 2A6M · Crystal Structure of the ISHp608 Transposase · 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 Q933Z0
- Elsewhere: RCSB PDB 2A6M · PDBe 2A6M · UniProt Q933Z0
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