Research workbench
Crystal structure of the protease CtpB(S309A) present in a resting state
Analyse Crystal structure of the protease CtpB(S309A) present in a resting state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4C2E
- Type
- protein
- Length
- 870 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.8
- Source
- BACILLUS SUBTILIS SUBSP. SUBTILIS STR. 168
- Molecule
- Carboxy-terminal processing protease ctpb
- EC
- 3.4.21.102
- UniProt
- O35002
- Pockets
- 6 · best druggability 0.72
Structure
x-ray diffraction · resolution 1.8 · 1 distinct chain · 34% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Carboxy-terminal processing protease ctpb (EC 3.4.21.102) | protein | 435 | 34% helix, 24% strand | O35002 |
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 644 | 0.72 | 0.79 | 55 | empty |
| 2 | 731 | 0.72 | 0.78 | 56 | empty |
| 3 | 601 | 0.70 | 0.78 | 81 | empty |
| 4 | 521 | 0.67 | 0.78 | 70 | empty |
| 5 | 61 | 0.36 | 0.79 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 2847 Ų buried · 44 hydrogen bonds · protein-protein
Compared structures
- 4C2E · Crystal structure of the protease CTPB(S309A) present in a resting state · the same entry in another collection · chain A against A, TM-score 1.00
- O35002 · AlphaFold monomer V2.0 prediction for carboxy-terminal processing protease ctpb (O35002) · a predicted model of the same protein · 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 O35002
- Elsewhere: RCSB PDB 4C2E · PDBe 4C2E · UniProt O35002
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