MolNFT v1 · #144954 · protein
The human nata (NAA10/NAA15) amino-terminal acetyltransferase complex
6C9M · N-alpha-acetyltransferase 15, nata auxiliary subunit: “The human nata (NAA10/NAA15) amino-terminal acetyltransferase complex”. X-ray diffraction, 2 ligands (ACE, IHP), 20 pockets (best druggability 0.71). MolNFT v1 #144954 on…
- PDB
- 6C9M
- Type
- protein
- Length
- 1,864 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-alpha-acetyltransferase 15, nata auxiliary subunit; N-alpha-acetyltransferase 10
- EC
- 2.3.1.255
- UniProt
- Q9BXJ9, P41227
- Ligands
- ACE, IHP
- Pockets
- 20 · best druggability 0.71
Structure
x-ray diffraction · 3 distinct chains · 72% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-alpha-acetyltransferase 15, nata auxiliary subunit | protein | 771 | 75% helix, 0% strand | Q9BXJ9 |
| B, D | N-alpha-acetyltransferase 10 (EC 2.3.1.255) | protein | 160 | 39% helix, 28% strand | P41227 |
| C | N-alpha-acetyltransferase 15, nata auxiliary subunit | protein | 773 | 76% helix, 0% strand | Q9BXJ9 |
Ligands and binding sites
- ACE · Acetyl group · ligand · 2 copies · chains A, B, C, D
- IHP · Inositol hexakisphosphate · ligand · 2 copies · chains A, B, C, D
- 1PE · Pentaethylene glycol · additive · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 563 | 0.71 | 0.79 | 59 | IHP |
| 2 | 566 | 0.70 | 0.79 | 47 | empty |
| 3 | 467 | 0.70 | 0.80 | 46 | IHP |
| 4 | 534 | 0.69 | 0.79 | 47 | empty |
| 5 | 363 | 0.64 | 0.79 | 41 | empty |
Interfaces
4 interfaces between chains.
- C–D · 2572 Ų buried · 40 hydrogen bonds · protein-protein
- A–B · 2542 Ų buried · 37 hydrogen bonds · protein-protein
- A–C · 1045 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 343 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 6C9M · The Human NatA (Naa10/Naa15) amino-terminal acetyltransferase complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q9BXJ9 · AlphaFold monomer V2.0 prediction for N-alpha-acetyltransferase 15, nata auxiliary… · a predicted model of the same protein · chain A against A, TM-score 0.98
- P41227 · AlphaFold monomer V2.0 prediction for N-alpha-acetyltransferase 10 (P41227) · a predicted model of the same protein · chain B against A, TM-score 0.96
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 Q9BXJ9
- Every structure of UniProt P41227
- Elsewhere: RCSB PDB 6C9M · PDBe 6C9M · UniProt Q9BXJ9 · UniProt P41227
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