Research workbench
Substrate induced remodeling of the active site regulates HTRA1 activity
Analyse Substrate induced remodeling of the active site regulates HTRA1 activity in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3NZI
- Type
- protein
- Length
- 215 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serine protease HTRA1; Citrate synthase
- EC
- 3.4.21.-
- UniProt
- Q92743, Q80X68
- Ligands
- B2V
- Pockets
- 1 · best druggability 0.34
Structure
x-ray diffraction · 2 distinct chains · 20% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serine protease HTRA1 (EC 3.4.21.-) | protein | 211 | 20% helix, 41% strand | Q92743 |
| B | Citrate synthase | protein | 4 | 0% helix, 25% strand | Q80X68 |
Ligands and binding sites
- B2V · Valine boronic acid · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 69 | 0.34 | 0.76 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 317 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 3NZI · Substrate induced remodeling of the active site regulates HtrA1 activity · the same entry in another collection · chain A against A, TM-score 1.00
- Q92743 · AlphaFold monomer V2.0 prediction for serine protease HTRA1 (Q92743) · a predicted model of the same protein · chain A against A, TM-score 0.95
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
- Every structure of UniProt Q80X68
- Elsewhere: RCSB PDB 3NZI · PDBe 3NZI · UniProt Q92743 · UniProt Q80X68
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