MolNFT v1 · #115369 · protein
Structural basis of H2A.Z recognition by YL1 histone chaperone component of SRCAP/SWR1 chromatin remodeling complex
5CHL · Vacuolar protein sorting-associated protein 72 homolog: “Structural basis of H2A.Z recognition by YL1 histone chaperone component of SRCAP/SWR1 chromatin remodeling…”. X-ray diffraction, 1 pocket (best druggability 0.37). MolNFT v1…
- PDB
- 5CHL
- Type
- protein
- Length
- 244 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vacuolar protein sorting-associated protein 72 homolog; Histone H2A.Z
- UniProt
- Q9VKM6, P0C0S5
- Pockets
- 1 · best druggability 0.37
Structure
x-ray diffraction · 2 distinct chains · 58% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vacuolar protein sorting-associated protein 72 homolog | protein | 68 | 28% helix, 1% strand | Q9VKM6 |
| B | Histone H2A.Z | protein | 176 | 70% helix, 4% strand | P0C0S5 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 82 | 0.37 | 0.76 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1937 Ų buried · 34 hydrogen bonds · protein-protein
Compared structures
- 5CHL · Structural basis of H2A.Z recognition by YL1 histone chaperone component of SRCAP/SWR1… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9VKM6 · AlphaFold monomer V2.0 prediction for vacuolar protein sorting- associated protein 72… · a predicted model of the same protein · chain A against A, TM-score 0.60
- P0C0S5 · AlphaFold monomer V2.0 prediction for histone H2A.Z (P0C0S5) · a predicted model of the same protein · chain B against A, TM-score 0.43
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 Q9VKM6
- Every structure of UniProt P0C0S5
- Elsewhere: RCSB PDB 5CHL · PDBe 5CHL · UniProt Q9VKM6 · UniProt P0C0S5
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