Research workbench
Crystal structure of human GCN5 histone acetyltransferase domain
Analyse Crystal structure of human GCN5 histone acetyltransferase domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5TRM
- Type
- protein
- Length
- 3,863 residues
- Chains
- 24
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone acetyltransferase KAT2A
- EC
- 2.3.1.48
- UniProt
- Q92830
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 16 distinct chains · 33% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, I | Histone acetyltransferase KAT2A (EC 2.3.1.48) | protein | 162 | 32% helix, 30% strand | Q92830 |
| W | Histone acetyltransferase KAT2A (EC 2.3.1.48) | protein | 160 | 30% helix, 31% strand | Q92830 |
| V, S, P, O | Histone acetyltransferase KAT2A (EC 2.3.1.48) | protein | 161 | 30% helix, 30% strand | Q92830 |
| U, G | Histone acetyltransferase KAT2A (EC 2.3.1.48) | protein | 164 | 34% helix, 28% strand | Q92830 |
| T | Histone acetyltransferase KAT2A (EC 2.3.1.48) | protein | 160 | 34% helix, 31% strand | Q92830 |
| R, F | Histone acetyltransferase KAT2A (EC 2.3.1.48) | protein | 162 | 33% helix, 30% strand | Q92830 |
| Q | Histone acetyltransferase KAT2A (EC 2.3.1.48) | protein | 156 | 35% helix, 30% strand | Q92830 |
| N, J | Histone acetyltransferase KAT2A (EC 2.3.1.48) | protein | 163 | 32% helix, 30% strand | Q92830 |
| M, X | Histone acetyltransferase KAT2A (EC 2.3.1.48) | protein | 160 | 34% helix, 29% strand | Q92830 |
| L | Histone acetyltransferase KAT2A (EC 2.3.1.48) | protein | 157 | 38% helix, 29% strand | Q92830 |
| K | Histone acetyltransferase KAT2A (EC 2.3.1.48) | protein | 160 | 33% helix, 30% strand | Q92830 |
| C | Histone acetyltransferase KAT2A (EC 2.3.1.48) | protein | 159 | 34% helix, 31% strand | Q92830 |
| B | Histone acetyltransferase KAT2A (EC 2.3.1.48) | protein | 161 | 32% helix, 30% strand | Q92830 |
| D | Histone acetyltransferase KAT2A (EC 2.3.1.48) | protein | 161 | 32% helix, 29% strand | Q92830 |
| E | Histone acetyltransferase KAT2A (EC 2.3.1.48) | protein | 163 | 34% helix, 30% strand | Q92830 |
| H | Histone acetyltransferase KAT2A (EC 2.3.1.48) | protein | 160 | 34% helix, 30% strand | Q92830 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 961 | 0.78 | 0.80 | 107 | empty |
| 2 | 1065 | 0.78 | 0.80 | 117 | empty |
| 3 | 815 | 0.76 | 0.80 | 102 | empty |
| 4 | 798 | 0.76 | 0.80 | 95 | empty |
| 5 | 747 | 0.75 | 0.80 | 96 | empty |
Interfaces
54 interfaces between chains.
- F–C · 819 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 809 Ų buried · 11 hydrogen bonds · protein-protein
- U–S · 802 Ų buried · 11 hydrogen bonds · protein-protein
- F–B · 792 Ų buried · 5 hydrogen bonds · protein-protein
- M–I · 789 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- Q92830 · AlphaFold monomer V2.0 prediction for histone acetyltransferase KAT2A (Q92830) · a predicted model of the same protein · chain K against A, TM-score 0.99
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 Q92830
- Elsewhere: RCSB PDB 5TRM · PDBe 5TRM · UniProt Q92830
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