MolNFT v1 · #13534 · protein
Three-dimensional structure of the immunodominant heat- shock protein chaperonin-10 of mycobacterium leprae
1LEP: “Three-dimensional structure of the immunodominant heat- shock protein chaperonin-10 of mycobacterium leprae”. X-ray diffraction, 6 pockets (best druggability 0.36). MolNFT v1 #13534 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1LEP
- Type
- protein
- Length
- 567 residues
- Chains
- 7
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperonin-10
- UniProt
- P24301
- Pockets
- 6 · best druggability 0.36
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G | Chaperonin-10 | protein | 81 | 0% helix, 0% strand | P24301 |
Pockets
6 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 93 | 0.36 | 0.73 | 28 | empty |
| 2 | 82 | 0.34 | 0.73 | 24 | empty |
| 3 | 70 | 0.31 | 0.72 | 25 | empty |
| 4 | 63 | 0.30 | 0.73 | 20 | empty |
| 5 | 50 | 0.30 | 0.74 | 15 | empty |
Interfaces
7 interfaces between chains.
- D–F · 121 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 118 Ų buried · 0 hydrogen bonds · protein-protein
- C–E · 114 Ų buried · 0 hydrogen bonds · protein-protein
- F–G · 109 Ų buried · 0 hydrogen bonds · protein-protein
- A–B · 107 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1LEP · Three-dimensional structure of the immunodominant heat-shock protein chaperonin-10 of… · the same entry in another collection · chain G against G, TM-score 1.00
- P24301 · AlphaFold monomer V2.0 prediction for 10 kda chaperonin (P24301) · a predicted model of the same protein · chain A against A, TM-score 0.85
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 P24301
- Elsewhere: RCSB PDB 1LEP · PDBe 1LEP · UniProt P24301
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