Research workbench
Arabidopsis thaliana NAA50 in complex with accoa
Analyse Arabidopsis thaliana NAA50 in complex with accoa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6YZZ
- Type
- protein
- Length
- 151 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-alpha-acetyltransferase 50
- UniProt
- Q9LFM3
- Ligands
- ACO
- Pockets
- 1 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-alpha-acetyltransferase 50 | protein | 151 | 34% helix, 38% strand | Q9LFM3 |
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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 435 | 0.62 | 0.76 | 41 | ACO |
Compared structures
- 6YZZ · Arabidopsis thaliana Naa50 in complex with AcCoA · 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 Q9LFM3
- Elsewhere: RCSB PDB 6YZZ · PDBe 6YZZ · UniProt Q9LFM3
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