Research workbench
Crystal structure of H2AM4>Z-H2B
Analyse Crystal structure of H2AM4>Z-H2B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7DLX
- Type
- protein
- Length
- 1,383 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone H2B,HISTONE H2A
- UniProt
- B3LG63, B3LG62
- Pockets
- 11 · best druggability 0.73
Structure
x-ray diffraction · 4 distinct chains · 73% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Histone H2B,HISTONE H2A | protein | 174 | 74% helix, 5% strand | B3LG63, B3LG62 |
| B | Histone H2B,HISTONE H2A | protein | 173 | 73% helix, 5% strand | B3LG63, B3LG62 |
| D, E, G, H | Histone H2B,HISTONE H2A | protein | 173 | 72% helix, 5% strand | B3LG63, B3LG62 |
| F | Histone H2B,HISTONE H2A | protein | 170 | 72% helix, 5% strand | B3LG63, B3LG62 |
Pockets
11 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 902 | 0.73 | 0.77 | 69 | empty |
| 2 | 841 | 0.69 | 0.75 | 76 | empty |
| 3 | 626 | 0.66 | 0.76 | 48 | empty |
| 4 | 589 | 0.65 | 0.76 | 63 | empty |
| 5 | 353 | 0.56 | 0.75 | 30 | empty |
Interfaces
13 interfaces between chains.
- A–C · 495 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 392 Ų buried · 4 hydrogen bonds · protein-protein
- F–H · 383 Ų buried · 2 hydrogen bonds · protein-protein
- E–G · 285 Ų buried · 1 hydrogen bond · protein-protein
- D–H · 277 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 7DLX · crystal structure of H2AM4>Z-H2B · the same entry in another collection · chain A against A, TM-score 1.00
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 B3LG63
- Every structure of UniProt B3LG62
- Elsewhere: RCSB PDB 7DLX · PDBe 7DLX · UniProt B3LG63 · UniProt B3LG62
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