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
- 3NUM
- Type
- protein
- Length
- 190 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serine protease HTRA1
- EC
- 3.4.21.-
- UniProt
- Q92743
Structure
x-ray diffraction · 1 distinct chain · 15% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serine protease HTRA1 (EC 3.4.21.-) | protein | 190 | 15% helix, 45% strand | Q92743 |
Compared structures
- 3NUM · 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 0.97
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 Q92743
- Elsewhere: RCSB PDB 3NUM · PDBe 3NUM · UniProt Q92743
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