Research workbench
A legionella acetyltransferase vipf
Analyse A legionella acetyltransferase vipf in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7C4G
- Type
- protein
- Length
- 270 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-acetyltransferase
- UniProt
- Q5C8M4
- Ligands
- COA, CLM
- Pockets
- 4 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acetyltransferase | protein | 270 | 33% helix, 32% strand | Q5C8M4 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 395 | 0.69 | 0.81 | 36 | COA |
| 2 | 201 | 0.46 | 0.74 | 26 | COA |
| 3 | 134 | 0.39 | 0.74 | 23 | CLM |
| 4 | 81 | 0.38 | 0.77 | 17 | empty |
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 Q5C8M4
- Elsewhere: RCSB PDB 7C4G · PDBe 7C4G · UniProt Q5C8M4
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