Research workbench
Crystal structure of a gnat superfamily acetyltransferase PA4794
Analyse Crystal structure of a gnat superfamily acetyltransferase PA4794 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4KUA
- Type
- protein
- Length
- 161 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gnat superfamily acetyltransferase PA4794
- UniProt
- Q9HV14
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gnat superfamily acetyltransferase PA4794 | protein | 161 | 34% helix, 37% strand | Q9HV14 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 345 | 0.69 | 0.82 | 38 | SO4, EDO |
| 2 | 56 | 0.31 | 0.76 | 17 | EDO |
Compared structures
- 4KUA · Crystal structure of a GNAT superfamily acetyltransferase PA4794 · 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 Q9HV14
- Elsewhere: RCSB PDB 4KUA · PDBe 4KUA · UniProt Q9HV14
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