Research workbench
Structure of the NOT1 superfamily homology domain from chaetomium thermophilum
Analyse Structure of the NOT1 superfamily homology domain from chaetomium thermophilum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4C0E
- Type
- protein
- Length
- 2,047 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NOT1
- UniProt
- G0SAL9
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 4 distinct chains · 69% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NOT1 | protein | 508 | 70% helix, 0% strand | G0SAL9 |
| B | NOT1 | protein | 505 | 70% helix, 0% strand | G0SAL9 |
| C | NOT1 | protein | 517 | 68% helix, 0% strand | G0SAL9 |
| D | NOT1 | protein | 517 | 67% helix, 0% strand | G0SAL9 |
Pockets
20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 693 | 0.81 | 0.85 | 46 | empty |
| 2 | 845 | 0.73 | 0.78 | 70 | empty |
| 3 | 57 | 0.66 | 0.95 | 21 | empty |
| 4 | 456 | 0.66 | 0.78 | 55 | empty |
| 5 | 493 | 0.63 | 0.76 | 46 | empty |
Interfaces
5 interfaces between chains.
- B–C · 2069 Ų buried · 12 hydrogen bonds · protein-protein
- A–B · 1312 Ų buried · 11 hydrogen bonds · protein-protein
- C–D · 810 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 99 Ų buried · 0 hydrogen bonds · protein-protein
- A–C · 43 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 43 modified (engineered).
Compared structures
- 4C0E · Structure of the NOT1 superfamily homology domain from Chaetomium thermophilum · 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 G0SAL9
- Elsewhere: RCSB PDB 4C0E · PDBe 4C0E · UniProt G0SAL9
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