Research workbench
Structure of an N-terminal fragment of leishmania sas-6 containing parts of its coiled coil domain, F257E mutant
Analyse Structure of an N-terminal fragment of leishmania sas-6 containing parts of its… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CKN
- Type
- protein
- Length
- 711 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sas-6
- UniProt
- E9AFQ5
- Pockets
- 10 · best druggability 0.55
Structure
x-ray diffraction · 4 distinct chains · 36% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sas-6 | protein | 178 | 37% helix, 42% strand | E9AFQ5 |
| B | Sas-6 | protein | 180 | 36% helix, 43% strand | E9AFQ5 |
| C | Sas-6 | protein | 181 | 38% helix, 43% strand | E9AFQ5 |
| D | Sas-6 | protein | 172 | 33% helix, 44% strand | E9AFQ5 |
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 102 | 0.55 | 0.84 | 21 | empty |
| 2 | 121 | 0.51 | 0.81 | 20 | empty |
| 3 | 114 | 0.51 | 0.81 | 20 | empty |
| 4 | 132 | 0.51 | 0.80 | 21 | empty |
| 5 | 116 | 0.41 | 0.77 | 17 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1446 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 1436 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 733 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 4CKN · Structure of an N-terminal fragment of Leishmania SAS-6 containing parts of its coiled… · 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 E9AFQ5
- Elsewhere: RCSB PDB 4CKN · PDBe 4CKN · UniProt E9AFQ5
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