Research workbench
HTRA1 inactive protease domain S328A with carasil mutation R274Q
Analyse HTRA1 inactive protease domain S328A with carasil mutation R274Q in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6Z0E
- Type
- protein
- Length
- 384 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serine protease HTRA1
- EC
- 3.4.21.-
- UniProt
- Q92743
- Ligands
- CA
- Pockets
- 1 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 14% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serine protease HTRA1 (EC 3.4.21.-) | protein | 196 | 13% helix, 41% strand | Q92743 |
| B | Serine protease HTRA1 (EC 3.4.21.-) | protein | 188 | 15% helix, 39% strand | Q92743 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 715 | 0.71 | 0.78 | 75 | empty |
Interfaces
1 interface between chains.
- A–B · 552 Ų buried · 6 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 6Z0E · PDBe 6Z0E · UniProt Q92743
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