Research workbench
Crystal structure of ASF1-Fab 12E complex
Analyse Crystal structure of ASF1-Fab 12E complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6AYZ
- Type
- protein
- Length
- 1,166 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fab heavy chain; Fab light chain; Histone chaperone ASF1
- UniProt
- P32447
- Pockets
- 16 · best druggability 0.59
Structure
x-ray diffraction · 6 distinct chains · 8% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Fab heavy chain | protein | 220 | 7% helix, 52% strand | — |
| C | Fab light chain | protein | 213 | 7% helix, 52% strand | — |
| D | Fab light chain | protein | 211 | 8% helix, 51% strand | — |
| M | Histone chaperone ASF1 | protein | 152 | 11% helix, 56% strand | P32447 |
| R | Fab heavy chain | protein | 221 | 5% helix, 52% strand | — |
| A | Histone chaperone ASF1 | protein | 149 | 10% helix, 54% strand | P32447 |
Pockets
16 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 421 | 0.59 | 0.75 | 48 | empty |
| 2 | 178 | 0.56 | 0.80 | 31 | empty |
| 3 | 63 | 0.55 | 0.89 | 21 | empty |
| 4 | 344 | 0.55 | 0.74 | 47 | empty |
| 5 | 218 | 0.54 | 0.78 | 23 | empty |
Interfaces
9 interfaces between chains.
- C–R · 2000 Ų buried · 12 hydrogen bonds · protein-protein
- B–D · 1952 Ų buried · 12 hydrogen bonds · protein-protein
- M–R · 851 Ų buried · 7 hydrogen bonds · protein-protein
- B–A · 751 Ų buried · 5 hydrogen bonds · protein-protein
- D–A · 634 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 9 disulfide (disulfide).
Compared structures
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 P32447
- Elsewhere: RCSB PDB 6AYZ · PDBe 6AYZ · UniProt P32447
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.