Research workbench
Crystal structure of CENAP1-H2A.Z-H2B complex
Analyse Crystal structure of CENAP1-H2A.Z-H2B complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6K0C
- Type
- protein
- Length
- 725 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone H2B 2,HISTONE H2A.V; Nucleosome assembly protein
- UniProt
- Q27894, Q27511, Q19007
- Pockets
- 9 · best druggability 0.75
Structure
x-ray diffraction · 3 distinct chains · 53% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D | Histone H2B 2,HISTONE H2A.V | protein | 179 | 71% helix, 3% strand | Q27894, Q27511 |
| A | Nucleosome assembly protein | protein | 277 | 45% helix, 16% strand | Q19007 |
| B | Nucleosome assembly protein | protein | 269 | 49% helix, 14% strand | Q19007 |
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 792 | 0.75 | 0.79 | 89 | empty |
| 2 | 236 | 0.62 | 0.82 | 42 | empty |
| 3 | 352 | 0.61 | 0.77 | 24 | empty |
| 4 | 182 | 0.46 | 0.74 | 18 | empty |
| 5 | 73 | 0.39 | 0.78 | 19 | empty |
Interfaces
3 interfaces between chains.
- A–B · 4589 Ų buried · 61 hydrogen bonds · protein-protein
- D–A · 575 Ų buried · 10 hydrogen bonds · protein-protein
- D–B · 378 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 6K0C · Crystal structure of ceNAP1-H2A.Z-H2B complex · the same entry in another collection · chain D against D, TM-score 1.00
- Q27894 · AlphaFold monomer V2.0 prediction for histone H2B 2 (Q27894) · a predicted model of the same protein · chain D against A, TM-score 0.47
- Q27511 · AlphaFold monomer V2.0 prediction for histone H2A.V (Q27511) · a predicted model of the same protein · chain D against A, TM-score 0.46
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 Q27894
- Every structure of UniProt Q27511
- Every structure of UniProt Q19007
- Elsewhere: RCSB PDB 6K0C · PDBe 6K0C · UniProt Q27894 · UniProt Q27511 · UniProt Q19007
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