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Crystal structure of an N-terminal HTATIP fragment
Analyse Crystal structure of an N-terminal HTATIP fragment in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4QQG
- Type
- protein
- Length
- 489 residues
- Chains
- 7
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.8
- Source
- Homo sapiens
- Molecule
- Histone acetyltransferase KAT5
- EC
- 2.3.1.48
- UniProt
- Q92993
- Ligands
- UNX
- Pockets
- 4 · best druggability 0.61
Structure
x-ray diffraction · resolution 2.8 · 6 distinct chains · 13% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone acetyltransferase KAT5 (EC 2.3.1.48) | protein | 71 | 13% helix, 38% strand | Q92993 |
| B | Histone acetyltransferase KAT5 (EC 2.3.1.48) | protein | 66 | 14% helix, 44% strand | Q92993 |
| C | Histone acetyltransferase KAT5 (EC 2.3.1.48) | protein | 70 | 13% helix, 39% strand | Q92993 |
| D, F | Histone acetyltransferase KAT5 (EC 2.3.1.48) | protein | 69 | 13% helix, 39% strand | Q92993 |
| E | Histone acetyltransferase KAT5 (EC 2.3.1.48) | protein | 72 | 13% helix, 38% strand | Q92993 |
| G | Histone acetyltransferase KAT5 (EC 2.3.1.48) | protein | 72 | 13% helix, 38% strand | Q92993 |
Ligands and binding sites
- UNX · Unknown atom or ion · ion · 13 copies · chains A, B, D, E, F, G, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 549 | 0.61 | 0.74 | 49 | UNX |
| 2 | 61 | 0.33 | 0.77 | 19 | empty |
| 3 | 67 | 0.31 | 0.74 | 12 | UNX |
| 4 | 58 | 0.29 | 0.74 | 13 | empty |
Interfaces
10 interfaces between chains.
- A–E · 576 Ų buried · 9 hydrogen bonds · protein-protein
- D–G · 561 Ų buried · 7 hydrogen bonds · protein-protein
- C–G · 384 Ų buried · 6 hydrogen bonds · protein-protein
- D–E · 206 Ų buried · 0 hydrogen bonds · protein-protein
- B–E · 124 Ų buried · 0 hydrogen bonds · protein-protein
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 Q92993
- Elsewhere: RCSB PDB 4QQG · PDBe 4QQG · UniProt Q92993
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