MolNFT v1 · #164409 · protein
Crystal structure of the tpr domain of KLC1 in complex with an engineered high-affinity cargo peptide.
6SWU: “Crystal structure of the tpr domain of KLC1 in complex with an engineered high-affinity cargo peptide.”. X-ray diffraction. MolNFT v1 #164409 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6SWU
- Type
- protein
- Length
- 1,718 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q5UE59
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 294 | — | Q5UE59 |
| B | — | protein | 288 | — | Q5UE59 |
| C | — | protein | 287 | — | Q5UE59 |
| D | — | protein | 287 | — | Q5UE59 |
| E | — | protein | 281 | — | Q5UE59 |
| F | — | protein | 281 | — | 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.
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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