Research workbench
The human nata (NAA10/NAA15) amino-terminal acetyltransferase complex bound to hypk
Analyse The human nata (NAA10/NAA15) amino-terminal acetyltransferase complex bound to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6C95
- Type
- protein
- Length
- 1,028 residues
- Chains
- 3
- 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, Q9NX55
- Ligands
- ACE, IHP
- Pockets
- 16 · best druggability 0.75
Structure
x-ray diffraction · 3 distinct chains · 68% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-alpha-acetyltransferase 15, nata auxiliary subunit | protein | 773 | 75% helix, 0% strand | Q9BXJ9 |
| B | N-alpha-acetyltransferase 10 (EC 2.3.1.255) | protein | 160 | 38% helix, 29% strand | P41227 |
| D | Huntingtin-interacting protein K | protein | 95 | 63% helix, 0% strand | Q9NX55 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 835 | 0.75 | 0.79 | 58 | empty |
| 2 | 570 | 0.75 | 0.82 | 58 | empty |
| 3 | 461 | 0.71 | 0.81 | 44 | IHP |
| 4 | 80 | 0.69 | 0.94 | 22 | ACE |
| 5 | 285 | 0.59 | 0.79 | 37 | empty |
Interfaces
3 interfaces between chains.
- A–B · 2521 Ų buried · 32 hydrogen bonds · protein-protein
- A–D · 1990 Ų buried · 19 hydrogen bonds · protein-protein
- B–D · 494 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 6C95 · The Human NatA (Naa10/Naa15) amino-terminal acetyltransferase complex bound to HYPK · the same entry in another collection · chain A against A, TM-score 1.00
- 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 0.98
- 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 0.96
- Q9NX55 · AlphaFold monomer V2.0 prediction for huntingtin-interacting protein K (Q9NX55) · a predicted model of the same protein · chain D against A, TM-score 0.61
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
- Every structure of UniProt Q9NX55
- Elsewhere: RCSB PDB 6C95 · PDBe 6C95 · UniProt Q9BXJ9 · UniProt P41227 · UniProt Q9NX55
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