Research workbench
Crystal structure of HAT1-HAT2-ASF1-H3-H4
Analyse Crystal structure of HAT1-HAT2-ASF1-H3-H4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7XAY
- Type
- protein
- Length
- 1,015 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Soluble cytochrome B562,HISTONE acetyltransferase type B catalytic subunit; Histone…
- EC
- 2.3.1.48
- UniProt
- Q12341, P39984, Q4WXX5, P61830, P02309
- Ligands
- COA
- Pockets
- 8 · best druggability 0.77
Structure
x-ray diffraction · 5 distinct chains · 25% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Soluble cytochrome B562,HISTONE acetyltransferase type B catalytic subunit (EC 2.3.1.48) | protein | 311 | 38% helix, 28% strand | Q12341 |
| B | Histone acetyltransferase type B subunit 2 | protein | 360 | 7% helix, 47% strand | P39984 |
| C | Histone chaperone ASF1 | protein | 154 | 9% helix, 53% strand | Q4WXX5 |
| D | Histone H3 | protein | 97 | 53% helix, 7% strand | P61830 |
| E | Histone H4 | protein | 93 | 49% helix, 9% strand | P02309 |
Ligands and binding sites
- COA · Coenzyme A · ligand · chains A, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 985 | 0.77 | 0.80 | 77 | empty |
| 2 | 860 | 0.75 | 0.79 | 101 | empty |
| 3 | 282 | 0.73 | 0.86 | 25 | empty |
| 4 | 190 | 0.56 | 0.79 | 26 | COA |
| 5 | 116 | 0.53 | 0.82 | 19 | empty |
Interfaces
8 interfaces between chains.
- D–E · 2175 Ų buried · 17 hydrogen bonds · protein-protein
- B–D · 1672 Ų buried · 21 hydrogen bonds · protein-protein
- A–E · 1090 Ų buried · 24 hydrogen bonds · protein-protein
- A–B · 916 Ų buried · 15 hydrogen bonds · protein-protein
- C–D · 789 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 7XAY · Crystal structure of Hat1-Hat2-Asf1-H3-H4 · the same entry in another collection · chain E against E, TM-score 1.00
- P39984 · AlphaFold monomer V2.0 prediction for histone acetyltransferase type B subunit 2 (P39984) · a predicted model of the same protein · chain B against A, TM-score 0.99
- Q12341 · AlphaFold monomer V2.0 prediction for histone acetyltransferase type B catalytic subunit… · a predicted model of the same protein · chain A against A, TM-score 0.98
- Q4WXX5 · AlphaFold monomer V2.0 prediction for histone chaperone ASF1 (Q4WXX5) · a predicted model of the same protein · chain C against A, TM-score 0.97
- P61830 · AlphaFold monomer V2.0 prediction for histone H3 (P61830) · a predicted model of the same protein · chain D against A, TM-score 0.73
- P02309 · AlphaFold monomer V2.0 prediction for histone H4 (P02309) · a predicted model of the same protein · chain E against A, TM-score 0.73
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 Q12341
- Every structure of UniProt P39984
- Every structure of UniProt Q4WXX5
- Every structure of UniProt P61830
- Every structure of UniProt P02309
- Elsewhere: RCSB PDB 7XAY · PDBe 7XAY · UniProt Q12341 · UniProt P39984 · UniProt Q4WXX5 · UniProt P61830 · UniProt P02309
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