MolNFT v1 · #181209 · protein
Structure of human ASF1A in complex with a TLK2 peptide
7LO0 · Histone chaperone ASF1A: “Structure of human ASF1A in complex with a TLK2 peptide”. X-ray diffraction, 11 pockets (best druggability 0.64). MolNFT v1 #181209 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7LO0
- Type
- protein
- Length
- 1,401 residues
- Chains
- 24
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone chaperone ASF1A; SERINE/THREONINE-protein kinase tousled-like 2
- EC
- 2.7.11.1
- UniProt
- Q9Y294, Q86UE8
- Pockets
- 11 · best druggability 0.64
Structure
x-ray diffraction · 10 distinct chains · 17% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, G | Histone chaperone ASF1A | protein | 154 | 12% helix, 50% strand | Q9Y294 |
| B, C | Histone chaperone ASF1A | protein | 153 | 12% helix, 56% strand | Q9Y294 |
| D | Histone chaperone ASF1A | protein | 151 | 10% helix, 54% strand | Q9Y294 |
| E, F, H | Histone chaperone ASF1A | protein | 152 | 12% helix, 52% strand | Q9Y294 |
| I, J, K | SERINE/THREONINE-protein kinase tousled-like 2 (EC 2.7.11.1) | protein | 15 | 80% helix, 0% strand | Q86UE8 |
| L, M | SERINE/THREONINE-protein kinase tousled-like 2 (EC 2.7.11.1) | protein | 16 | 69% helix, 0% strand | Q86UE8 |
| N | SERINE/THREONINE-protein kinase tousled-like 2 (EC 2.7.11.1) | protein | 18 | 67% helix, 0% strand | Q86UE8 |
| O, P | SERINE/THREONINE-protein kinase tousled-like 2 (EC 2.7.11.1) | protein | 14 | 86% helix, 0% strand | Q86UE8 |
| Q, T, U, V, W, X, Y | SERINE/THREONINE-protein kinase tousled-like 2 (EC 2.7.11.1) | protein | 7 | 0% helix, 29% strand | Q86UE8 |
| R | SERINE/THREONINE-protein kinase tousled-like 2 (EC 2.7.11.1) | protein | 8 | 0% helix, 25% strand | Q86UE8 |
Pockets
11 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 179 | 0.64 | 0.84 | 28 | empty |
| 2 | 75 | 0.46 | 0.82 | 19 | empty |
| 3 | 65 | 0.45 | 0.82 | 18 | empty |
| 4 | 143 | 0.43 | 0.75 | 20 | empty |
| 5 | 133 | 0.42 | 0.75 | 26 | empty |
Interfaces
29 interfaces between chains.
- F–N · 759 Ų buried · 10 hydrogen bonds · protein-protein
- E–M · 677 Ų buried · 12 hydrogen bonds · protein-protein
- C–K · 676 Ų buried · 8 hydrogen bonds · protein-protein
- D–L · 669 Ų buried · 11 hydrogen bonds · protein-protein
- H–P · 662 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 7LO0 · Structure of human ASF1a in complex with a TLK2 peptide · the same entry in another collection · chain K against K, 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 Q9Y294
- Every structure of UniProt Q86UE8
- Elsewhere: RCSB PDB 7LO0 · PDBe 7LO0 · UniProt Q9Y294 · UniProt Q86UE8
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