Research workbench
Htra proteases are activated by a conserved mechanism that can be triggered by distinct molecular cues
Analyse Htra proteases are activated by a conserved mechanism that can be triggered by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MH7
- Type
- protein
- Length
- 402 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protease do; 5-mer peptide
- EC
- 3.4.21.-
- UniProt
- P0C0V0
- Pockets
- 6 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 18% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protease do (EC 3.4.21.-) | protein | 392 | 19% helix, 40% strand | P0C0V0 |
| B, C | 5-mer peptide | protein | 5 | 0% helix, 60% strand | — |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 210 | 0.62 | 0.82 | 27 | empty |
| 2 | 173 | 0.53 | 0.79 | 23 | empty |
| 3 | 90 | 0.43 | 0.79 | 21 | empty |
| 4 | 91 | 0.41 | 0.78 | 16 | empty |
| 5 | 76 | 0.29 | 0.73 | 16 | empty |
Interfaces
2 interfaces between chains.
- A–B · 347 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 305 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 13 modified (engineered).
Compared structures
- 3MH7 · HtrA proteases are activated by a conserved mechanism that can be triggered by distinct… · the same entry in another collection · chain A against A, TM-score 1.00
- P0C0V0 · AlphaFold monomer V2.0 prediction for periplasmic serine endoprotease degp (P0C0V0) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P0C0V0
- Elsewhere: RCSB PDB 3MH7 · PDBe 3MH7 · UniProt P0C0V0
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