Research workbench
HTRA1 catalytic domain, apo form
Analyse HTRA1 catalytic domain, apo form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TJN
- Type
- protein
- Length
- 574 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serine protease HTRA1
- EC
- 3.4.21.-
- UniProt
- Q92743
- Pockets
- 4 · best druggability 0.63
Structure
x-ray diffraction · 3 distinct chains · 17% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serine protease HTRA1 (EC 3.4.21.-) | protein | 190 | 17% helix, 46% strand | Q92743 |
| B | Serine protease HTRA1 (EC 3.4.21.-) | protein | 197 | 19% helix, 44% strand | Q92743 |
| D | Serine protease HTRA1 (EC 3.4.21.-) | protein | 187 | 16% helix, 41% strand | Q92743 |
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 | 352 | 0.63 | 0.78 | 29 | empty |
| 2 | 110 | 0.53 | 0.83 | 21 | empty |
| 3 | 71 | 0.32 | 0.75 | 12 | empty |
| 4 | 55 | 0.28 | 0.74 | 13 | empty |
Interfaces
2 interfaces between chains.
- A–B · 296 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 264 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
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 Q92743
- Elsewhere: RCSB PDB 3TJN · PDBe 3TJN · UniProt Q92743
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