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Structure of an N-terminal fragment of leishmania sas-6 that contains part of its coiled coil domain
Analyse Structure of an N-terminal fragment of leishmania sas-6 that contains part of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CKP
- Type
- protein
- Length
- 1,109 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sas-6
- UniProt
- E9AFQ5
- Pockets
- 20 · best druggability 0.56
Structure
x-ray diffraction · 6 distinct chains · 35% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sas-6 | protein | 176 | 32% helix, 42% strand | E9AFQ5 |
| B | Sas-6 | protein | 177 | 32% helix, 43% strand | E9AFQ5 |
| C | Sas-6 | protein | 189 | 36% helix, 40% strand | E9AFQ5 |
| D | Sas-6 | protein | 188 | 37% helix, 40% strand | E9AFQ5 |
| E | Sas-6 | protein | 190 | 36% helix, 40% strand | E9AFQ5 |
| F | Sas-6 | protein | 189 | 37% helix, 39% strand | E9AFQ5 |
Pockets
20 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 155 | 0.56 | 0.82 | 22 | empty |
| 2 | 145 | 0.55 | 0.82 | 23 | empty |
| 3 | 135 | 0.54 | 0.82 | 21 | empty |
| 4 | 142 | 0.52 | 0.80 | 21 | empty |
| 5 | 123 | 0.51 | 0.81 | 21 | empty |
Interfaces
5 interfaces between chains.
- E–F · 1558 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 1507 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 1155 Ų buried · 6 hydrogen bonds · protein-protein
- D–E · 939 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 936 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 4CKP · Structure of an N-terminal fragment of Leishmania SAS-6 that contains part 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 4CKP · PDBe 4CKP · UniProt E9AFQ5
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