Research workbench
Structural basis for the co-chaperone relationship of snasp and ASF1B
Analyse Structural basis for the co-chaperone relationship of snasp and ASF1B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7V1M
- Type
- protein
- Length
- 1,022 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone H3.3; Histone H4; Histone chaperone ASF1B; Isoform 2 of nuclear autoantigenic…
- UniProt
- P84243, P62805, Q9NVP2
- Pockets
- 17 · best druggability 0.81
Structure
x-ray diffraction · 7 distinct chains · 63% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Histone H3.3 | protein | 86 | 60% helix, 5% strand | P84243 |
| C | Histone H4 | protein | 80 | 59% helix, 9% strand | P62805 |
| D, F | Histone chaperone ASF1B | protein | 154 | 12% helix, 53% strand | Q9NVP2 |
| A | Histone H3.3 | protein | 75 | 71% helix, 3% strand | P84243 |
| E | Histone H4 | protein | 78 | 58% helix, 6% strand | P62805 |
| G | Isoform 2 of nuclear autoantigenic sperm protein | protein | 195 | 83% helix, 0% strand | — |
| H | Isoform 2 of nuclear autoantigenic sperm protein | protein | 200 | 84% helix, 0% strand | — |
Pockets
17 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 993 | 0.81 | 0.82 | 88 | empty |
| 2 | 373 | 0.71 | 0.82 | 55 | empty |
| 3 | 512 | 0.71 | 0.80 | 40 | empty |
| 4 | 408 | 0.69 | 0.81 | 44 | empty |
| 5 | 402 | 0.66 | 0.79 | 43 | empty |
Interfaces
13 interfaces between chains.
- B–C · 2152 Ų buried · 11 hydrogen bonds · protein-protein
- A–E · 2059 Ų buried · 7 hydrogen bonds · protein-protein
- G–H · 1042 Ų buried · 12 hydrogen bonds · protein-protein
- A–F · 894 Ų buried · 9 hydrogen bonds · protein-protein
- B–D · 889 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 7V1M · Structural basis for the co-chaperone relationship of sNASP and ASF1b · the same entry in another collection · chain H against H, TM-score 1.00
- Q9NVP2 · AlphaFold monomer V2.0 prediction for histone chaperone ASF1B (Q9NVP2) · a predicted model of the same protein · chain D against A, TM-score 0.98
- P84243 · AlphaFold monomer V2.0 prediction for histone H3.3 (P84243) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 P84243
- Every structure of UniProt P62805
- Every structure of UniProt Q9NVP2
- Elsewhere: RCSB PDB 7V1M · PDBe 7V1M · UniProt P84243 · UniProt P62805 · UniProt Q9NVP2
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.