Research workbench
Crystal structure of a GCN5-related N-acetyltransferase from brucella melitensis
Analyse Crystal structure of a GCN5-related N-acetyltransferase from brucella melitensis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TCV
- Type
- protein
- Length
- 444 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GCN5-related N-acetyltransferase
- EC
- 2.3.1.5
- UniProt
- Q2YIN4
- Pockets
- 2 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GCN5-related N-acetyltransferase (EC 2.3.1.5) | protein | 221 | 37% helix, 30% strand | Q2YIN4 |
| B | GCN5-related N-acetyltransferase (EC 2.3.1.5) | protein | 223 | 37% helix, 30% strand | Q2YIN4 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 603 | 0.70 | 0.78 | 68 | empty |
| 2 | 358 | 0.67 | 0.80 | 41 | empty |
Interfaces
1 interface between chains.
- A–B · 1227 Ų buried · 35 hydrogen bonds · protein-protein
Compared structures
- 3TCV · Crystal structure of a GCN5-related N-acetyltransferase from Brucella melitensis · 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 Q2YIN4
- Elsewhere: RCSB PDB 3TCV · PDBe 3TCV · UniProt Q2YIN4
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.