MolNFT v1 · #141546 · protein
The structural basis of histone CHAPERONEVPS75
5ZB5 · Nap family histone chaperone VPS75: “The structural basis of histone CHAPERONEVPS75”. X-ray diffraction, 1 pocket (best druggability 0.75). MolNFT v1 #141546 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5ZB5
- Type
- protein
- Length
- 385 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nap family histone chaperone VPS75
- UniProt
- M1JYC8
- Pockets
- 1 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nap family histone chaperone VPS75 | protein | 196 | 48% helix, 14% strand | M1JYC8 |
| B | Nap family histone chaperone VPS75 | protein | 189 | 49% helix, 14% strand | M1JYC8 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 905 | 0.75 | 0.78 | 77 | PEG |
Interfaces
1 interface between chains.
- A–B · 1444 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 5ZB5 · The structural basis of histone chaperoneVps75 · 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 M1JYC8
- Elsewhere: RCSB PDB 5ZB5 · PDBe 5ZB5 · UniProt M1JYC8
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