Research workbench
Crystal structure of the macro domain of human core histone H2A
Analyse Crystal structure of the macro domain of human core histone H2A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XD7
- Type
- protein
- Length
- 764 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Core histone macro-H2A.2
- UniProt
- Q9P0M6
- Pockets
- 10 · best druggability 0.58
Structure
x-ray diffraction · 3 distinct chains · 41% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Core histone macro-H2A.2 | protein | 192 | 41% helix, 21% strand | Q9P0M6 |
| C | Core histone macro-H2A.2 | protein | 193 | 40% helix, 21% strand | Q9P0M6 |
| D | Core histone macro-H2A.2 | protein | 187 | 42% helix, 21% strand | Q9P0M6 |
Pockets
10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 254 | 0.58 | 0.79 | 29 | empty |
| 2 | 77 | 0.57 | 0.87 | 19 | empty |
| 3 | 68 | 0.54 | 0.87 | 20 | empty |
| 4 | 104 | 0.52 | 0.82 | 23 | empty |
| 5 | 58 | 0.52 | 0.87 | 19 | empty |
Interfaces
3 interfaces between chains.
- A–C · 510 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 169 Ų buried · 0 hydrogen bonds · protein-protein
- C–D · 143 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 Q9P0M6
- Elsewhere: RCSB PDB 2XD7 · PDBe 2XD7 · UniProt Q9P0M6
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