Research workbench
The crystal structure of ct mutant
Analyse The crystal structure of ct mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5DLK
- Type
- protein
- Length
- 1,766 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tqaa
- UniProt
- F1CWE4
- Pockets
- 20 · best druggability 0.74
Structure
x-ray diffraction · 4 distinct chains · 34% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tqaa | protein | 443 | 35% helix, 24% strand | F1CWE4 |
| B | Tqaa | protein | 442 | 35% helix, 24% strand | F1CWE4 |
| C | Tqaa | protein | 440 | 34% helix, 24% strand | F1CWE4 |
| D | Tqaa | protein | 441 | 33% helix, 24% strand | F1CWE4 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 18 copies · chains A, B, C, D
- DMS · Dimethyl sulfoxide · additive · 8 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 393 | 0.74 | 0.84 | 45 | EDO, DMS |
| 2 | 370 | 0.73 | 0.84 | 48 | DMS |
| 3 | 377 | 0.72 | 0.83 | 46 | EDO, DMS |
| 4 | 374 | 0.71 | 0.82 | 46 | EDO, DMS |
| 5 | 460 | 0.67 | 0.78 | 51 | EDO |
Interfaces
3 interfaces between chains.
- A–B · 499 Ų buried · 8 hydrogen bonds · protein-protein
- B–D · 175 Ų buried · 1 hydrogen bond · protein-protein
- A–C · 170 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 5DLK · The crystal structure of CT mutant · 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 F1CWE4
- Elsewhere: RCSB PDB 5DLK · PDBe 5DLK · UniProt F1CWE4
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