Research workbench
A legionella acetyltransferase effector vipf
Analyse A legionella acetyltransferase effector vipf in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7C4E
- Type
- protein
- Length
- 292 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-acetyltransferase
- UniProt
- Q5C8M4
- Ligands
- ACO
- Pockets
- 3 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acetyltransferase | protein | 292 | 33% helix, 33% strand | Q5C8M4 |
Ligands and binding sites
- ACO · Acetyl coenzyme *A · ligand · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 465 | 0.74 | 0.82 | 37 | ACO |
| 2 | 402 | 0.57 | 0.74 | 45 | ACO |
| 3 | 83 | 0.35 | 0.75 | 16 | 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 7C4E · PDBe 7C4E · UniProt Q5C8M4
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