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Crystal structure of trypanosoma brucei acetyltransferase, TB11.01.2886
Analyse Crystal structure of trypanosoma brucei acetyltransferase, TB11.01.2886 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FB3
- Type
- protein
- Length
- 291 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-acetyltransferase
- UniProt
- Q383G8
- Pockets
- 4 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acetyltransferase | protein | 142 | 33% helix, 36% strand | Q383G8 |
| B | N-acetyltransferase | protein | 149 | 34% helix, 32% strand | Q383G8 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 666 | 0.74 | 0.80 | 68 | empty |
| 2 | 63 | 0.43 | 0.81 | 14 | empty |
| 3 | 58 | 0.29 | 0.74 | 17 | empty |
| 4 | 51 | 0.27 | 0.74 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 2819 Ų buried · 46 hydrogen bonds · protein-protein
Compared structures
- 3FB3 · Crystal Structure of Trypanosoma Brucei Acetyltransferase, Tb11.01.2886 · 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 Q383G8
- Elsewhere: RCSB PDB 3FB3 · PDBe 3FB3 · UniProt Q383G8
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