Research workbench
Crystal structure of the tpr domain of KLC1 in complex with an engineered high-affinity cargo peptide.
Analyse Crystal structure of the tpr domain of KLC1 in complex with an engineered… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SWU
- Type
- protein
- Length
- 1,718 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kinesin light chain 1,KINESIN light chain 1,TPR domain of kinesin light chain 1 in…
- UniProt
- Q5UE59
- Pockets
- 20 · best druggability 0.79
Structure
x-ray diffraction · 6 distinct chains · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kinesin light chain 1,KINESIN light chain 1,TPR domain of kinesin light chain 1 in complex with an engineered high-affinity cargo peptide of sequence tvfttediyewddsai | protein | 294 | 75% helix, 0% strand | Q5UE59 |
| B | Kinesin light chain 1,KINESIN light chain 1,TPR domain of kinesin light chain 1 in complex with an engineered high-affinity cargo peptide of sequence tvfttediyewddsai | protein | 288 | 77% helix, 1% strand | Q5UE59 |
| C | Kinesin light chain 1,KINESIN light chain 1,TPR domain of kinesin light chain 1 in complex with an engineered high-affinity cargo peptide of sequence tvfttediyewddsai | protein | 287 | 77% helix, 0% strand | Q5UE59 |
| D | Kinesin light chain 1,KINESIN light chain 1,TPR domain of kinesin light chain 1 in complex with an engineered high-affinity cargo peptide of sequence tvfttediyewddsai | protein | 287 | 76% helix, 0% strand | Q5UE59 |
| E | Kinesin light chain 1,KINESIN light chain 1,TPR domain of kinesin light chain 1 in complex with an engineered high-affinity cargo peptide of sequence tvfttediyewddsai | protein | 281 | 76% helix, 0% strand | Q5UE59 |
| F | Kinesin light chain 1,KINESIN light chain 1,TPR domain of kinesin light chain 1 in complex with an engineered high-affinity cargo peptide of sequence tvfttediyewddsai | protein | 281 | 76% helix, 0% strand | Q5UE59 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 9 copies · chains C, A, B, D, E, F
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1050 | 0.79 | 0.80 | 104 | empty |
| 2 | 851 | 0.77 | 0.80 | 59 | EDO |
| 3 | 680 | 0.76 | 0.81 | 68 | empty |
| 4 | 596 | 0.75 | 0.81 | 63 | empty |
| 5 | 316 | 0.65 | 0.81 | 33 | empty |
Interfaces
8 interfaces between chains.
- C–D · 2270 Ų buried · 29 hydrogen bonds · protein-protein
- A–B · 2268 Ų buried · 35 hydrogen bonds · protein-protein
- E–F · 2011 Ų buried · 25 hydrogen bonds · protein-protein
- A–F · 595 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 351 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6SWU · Crystal structure of the TPR domain of KLC1 in complex with an engineered high-affinity… · 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 Q5UE59
- Elsewhere: RCSB PDB 6SWU · PDBe 6SWU · UniProt Q5UE59
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