Research workbench
Crystal structure of NAA10 (ARD1) bound to accoa
Analyse Crystal structure of NAA10 (ARD1) bound to accoa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4KVX
- Type
- protein
- Length
- 304 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-terminal acetyltransferase a complex catalytic subunit ARD1
- EC
- 2.3.1.88
- UniProt
- Q9UTI3
- Ligands
- ACO
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | N-terminal acetyltransferase a complex catalytic subunit ARD1 (EC 2.3.1.88) | protein | 152 | 36% helix, 29% strand | Q9UTI3 |
Ligands and binding sites
- ACO · Acetyl coenzyme *A · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 349 | 0.70 | 0.83 | 41 | ACO |
| 2 | 363 | 0.69 | 0.82 | 38 | ACO |
| 3 | 324 | 0.57 | 0.76 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 109 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 modified (engineered).
Compared structures
- 4KVX · Crystal structure of Naa10 (Ard1) bound to AcCoA · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UTI3 · AlphaFold monomer V2.0 prediction for N-terminal acetyltransferase a complex catalytic… · a predicted model of the same protein · chain A against A, TM-score 0.91
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 Q9UTI3
- Elsewhere: RCSB PDB 4KVX · PDBe 4KVX · UniProt Q9UTI3
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