Research workbench
Crystal structure of human NAA60 in complex with CoA
Analyse Crystal structure of human NAA60 in complex with CoA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5HH0
- Type
- protein
- Length
- 195 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-alpha-acetyltransferase 60
- EC
- 2.3.1.48, 2.3.1.88
- UniProt
- Q9H7X0
- Ligands
- COA
- Pockets
- 1 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-alpha-acetyltransferase 60 (EC 2.3.1.48, 2.3.1.88) | protein | 195 | 37% helix, 32% strand | Q9H7X0 |
Ligands and binding sites
- COA · 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 | 586 | 0.72 | 0.80 | 51 | COA |
Compared structures
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 Q9H7X0
- Elsewhere: RCSB PDB 5HH0 · PDBe 5HH0 · UniProt Q9H7X0
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