Research workbench
The structure of a GCN5-related N-acetyltransferase from kribbella flavida
Analyse The structure of a GCN5-related N-acetyltransferase from kribbella flavida in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4H89
- Type
- protein
- Length
- 168 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GCN5-related N-acetyltransferase
- UniProt
- D2Q3N2
- Pockets
- 1 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GCN5-related N-acetyltransferase | protein | 168 | 33% helix, 35% strand | D2Q3N2 |
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 | 315 | 0.65 | 0.80 | 49 | empty |
Modifications
Observed in the structure: 5 modified (engineered).
Compared structures
- 4H89 · The Structure of a GCN5-Related N-Acetyltransferase from Kribbella flavida · 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 D2Q3N2
- Elsewhere: RCSB PDB 4H89 · PDBe 4H89 · UniProt D2Q3N2
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