MolNFT v1 · #71538 · protein
Htra proteases are activated by a conserved mechanism that can be triggered by distinct molecular cues
3MH6 · Protease do: “Htra proteases are activated by a conserved mechanism that can be triggered by distinct molecular cues”. X-ray diffraction, 1 ligand (DFP), 8 pockets (best druggability 0.75). MolNFT v1 #71538 on GenesisL1: 3D…
- PDB
- 3MH6
- Type
- protein
- Length
- 392 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protease do
- EC
- 3.4.21.-
- UniProt
- P0C0V0
- Ligands
- DFP
- Pockets
- 8 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protease do (EC 3.4.21.-) | protein | 392 | 17% helix, 37% strand | P0C0V0 |
Ligands and binding sites
- DFP · Diisopropyl phosphonate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 65 | 0.75 | 0.98 | 24 | empty |
| 2 | 365 | 0.63 | 0.79 | 50 | empty |
| 3 | 137 | 0.54 | 0.81 | 17 | empty |
| 4 | 128 | 0.50 | 0.80 | 16 | empty |
| 5 | 56 | 0.34 | 0.78 | 16 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 3MH6 · 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 0.96
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 3MH6 · PDBe 3MH6 · UniProt P0C0V0
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