MolNFT v1 · #149357 · protein
Crystal structure of the macro domain of human MACROH2A2
6FY5 · Core histone macro-H2A.2: “Crystal structure of the macro domain of human MACROH2A2”. X-ray diffraction, 3 pockets (best druggability 0.69). MolNFT v1 #149357 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6FY5
- Type
- protein
- Length
- 391 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Core histone macro-H2A.2
- UniProt
- Q9P0M6
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Core histone macro-H2A.2 | protein | 198 | 39% helix, 22% strand | Q9P0M6 |
| B | Core histone macro-H2A.2 | protein | 193 | 40% helix, 21% strand | Q9P0M6 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 3 copies · chains A, B
- ACT · Acetate ion · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 121 | 0.69 | 0.90 | 27 | EDO |
| 2 | 61 | 0.42 | 0.82 | 13 | EDO |
| 3 | 87 | 0.39 | 0.77 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 379 Ų buried · 6 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 6FY5 · PDBe 6FY5 · UniProt Q9P0M6
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