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The 3.0 a resolution structure of caseinolytic clp protease 1 from mycobacterium tuberculosis
Analyse The 3.0 a resolution structure of caseinolytic clp protease 1 from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2C8T
- Type
- protein
- Length
- 2,394 residues
- Chains
- 14
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent clp protease proteolytic subunit 1
- EC
- 3.4.21.92
- UniProt
- P0A526
- Pockets
- 20 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N | ATP-dependent clp protease proteolytic subunit 1 (EC 3.4.21.92) | protein | 171 | 50% helix, 20% strand | P0A526 |
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 | 287 | 0.52 | 0.74 | 46 | empty |
| 2 | 275 | 0.51 | 0.74 | 46 | empty |
| 3 | 285 | 0.51 | 0.74 | 47 | empty |
| 4 | 82 | 0.50 | 0.83 | 16 | empty |
| 5 | 102 | 0.50 | 0.82 | 21 | empty |
Interfaces
21 interfaces between chains.
- D–E · 1512 Ų buried · 13 hydrogen bonds · protein-protein
- K–L · 1505 Ų buried · 14 hydrogen bonds · protein-protein
- A–G · 1501 Ų buried · 14 hydrogen bonds · protein-protein
- J–K · 1499 Ų buried · 11 hydrogen bonds · protein-protein
- M–N · 1493 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 2C8T · The 3.0 A Resolution Structure of Caseinolytic Clp Protease 1 from Mycobacterium… · 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 P0A526
- Elsewhere: RCSB PDB 2C8T · PDBe 2C8T · UniProt P0A526
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