Research workbench
A glutamic acid specific serine protease utilizes a novel histidine triad in substrate binding
Analyse A glutamic acid specific serine protease utilizes a novel histidine triad in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HPG
- Type
- protein
- Length
- 191 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamic acid specific protease; Boc-ala-ala-pro-glu peptide
- EC
- 3.4.21.82
- UniProt
- Q54211
- Ligands
- BOC
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamic acid specific protease (EC 3.4.21.82) | protein | 187 | 6% helix, 53% strand | Q54211 |
| B | Boc-ala-ala-pro-glu peptide | protein | 4 | 0% helix, 50% strand | — |
Ligands and binding sites
- BOC · Tert-butyl hydrogen carbonate · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 340 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide, 1 covalent (disulfide, covalent ligand).
Compared structures
- 1HPG · A glutamic acid specific serine protease utilizes a novel histidine triad in substrate… · the same entry in another collection · chain A against A, TM-score 1.00
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 Q54211
- Elsewhere: RCSB PDB 1HPG · PDBe 1HPG · UniProt Q54211
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.