Research workbench
Crystal structure of vipf from legionella hackeliae in complex with acetyl-CoA
Analyse Crystal structure of vipf from legionella hackeliae in complex with acetyl-CoA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6WQB
- Type
- protein
- Length
- 290 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-terminal acetyltransferase, gnat family
- UniProt
- A0A0A8UKD4
- Ligands
- ACO
- Pockets
- 2 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-terminal acetyltransferase, gnat family | protein | 290 | 35% helix, 34% strand | A0A0A8UKD4 |
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
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 | 292 | 0.69 | 0.83 | 30 | ACO |
| 2 | 587 | 0.62 | 0.74 | 52 | ACO |
Compared structures
- 6WQB · Crystal structure of VipF from Legionella hackeliae in complex with acetyl-CoA · 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 A0A0A8UKD4
- Elsewhere: RCSB PDB 6WQB · PDBe 6WQB · UniProt A0A0A8UKD4
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