Research workbench
Crystal structure of the protease ctpb in an active state
Analyse Crystal structure of the protease ctpb in an active state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4C2C
- Type
- protein
- Length
- 440 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carboxy-terminal processing protease ctpb; PEPTIDE1; PEPTIDE2
- UniProt
- O35002
- Pockets
- 4 · best druggability 0.68
Structure
x-ray diffraction · 3 distinct chains · 33% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carboxy-terminal processing protease ctpb | protein | 433 | 34% helix, 24% strand | O35002 |
| B | PEPTIDE1 | protein | 3 | 0% helix, 33% strand | — |
| C | PEPTIDE2 | protein | 4 | 0% helix, 50% strand | — |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 705 | 0.68 | 0.76 | 64 | empty |
| 2 | 298 | 0.54 | 0.75 | 40 | empty |
| 3 | 57 | 0.39 | 0.80 | 16 | empty |
| 4 | 63 | 0.33 | 0.76 | 11 | empty |
Interfaces
2 interfaces between chains.
- A–C · 340 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 262 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
- 4C2C · Crystal structure of the protease CtpB in an active 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 0.80
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 4C2C · PDBe 4C2C · UniProt O35002
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