Research workbench
The structure of clpp at 2.3 ångström resolution suggests a model for ATP-dependent proteolysis
Analyse The structure of clpp at 2.3 ångström resolution suggests a model for… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TYF
- Type
- protein
- Length
- 2,562 residues
- Chains
- 14
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Clp peptidase
- EC
- 3.4.21.92
- UniProt
- P0A6G7
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N | Clp peptidase (EC 3.4.21.92) | protein | 183 | 46% helix, 23% strand | P0A6G7 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 966 | 0.78 | 0.80 | 114 | empty |
| 2 | 769 | 0.76 | 0.80 | 75 | empty |
| 3 | 754 | 0.76 | 0.81 | 91 | empty |
| 4 | 732 | 0.76 | 0.81 | 76 | empty |
| 5 | 841 | 0.76 | 0.80 | 94 | empty |
Interfaces
40 interfaces between chains.
- C–D · 1774 Ų buried · 22 hydrogen bonds · protein-protein
- K–L · 1750 Ų buried · 22 hydrogen bonds · protein-protein
- F–G · 1739 Ų buried · 25 hydrogen bonds · protein-protein
- A–G · 1737 Ų buried · 20 hydrogen bonds · protein-protein
- L–M · 1729 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 1TYF · The structure of clpp at 2.3 ångström resolution suggests a model for ATP-dependent… · the same entry in another collection · chain K against K, 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 P0A6G7
- Elsewhere: RCSB PDB 1TYF · PDBe 1TYF · UniProt P0A6G7
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