Research workbench
The crystal structure of campylobacter jejuni N-acetyltransferase pseh in complex with acetyl coenzyme a
Analyse The crystal structure of campylobacter jejuni N-acetyltransferase pseh in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4XPL
- Type
- protein
- Length
- 141 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-acetyltransferase, pseh
- UniProt
- K0HK73
- Ligands
- ACO
- Pockets
- 1 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acetyltransferase, pseh | protein | 141 | 37% helix, 34% strand | K0HK73 |
Ligands and binding sites
- ACO · Acetyl coenzyme *A · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 256 | 0.49 | 0.73 | 35 | ACO |
Compared structures
- 4XPL · The crystal structure of Campylobacter jejuni N-acetyltransferase PseH in complex with… · 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 K0HK73
- Elsewhere: RCSB PDB 4XPL · PDBe 4XPL · UniProt K0HK73
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