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Crystal structure of the N-terminal catalytic domain of TP901-1 integrase
Analyse Crystal structure of the N-terminal catalytic domain of TP901-1 integrase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BVP
- Type
- protein
- Length
- 266 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TP901-1 integrase
- UniProt
- Q38184
- Pockets
- 1 · best druggability 0.53
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TP901-1 integrase | protein | 136 | 51% helix, 20% strand | Q38184 |
| B | TP901-1 integrase | protein | 130 | 52% helix, 21% strand | Q38184 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 127 | 0.53 | 0.81 | 33 | empty |
Interfaces
1 interface between chains.
- A–B · 644 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 3BVP · Crystal Structure of the N-terminal Catalytic Domain of TP901-1 Integrase · 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 Q38184
- Elsewhere: RCSB PDB 3BVP · PDBe 3BVP · UniProt Q38184
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