Research workbench
Crystal structure of wild-type alpha-lytic protease at 1.6 a, pH 5.14
Analyse Crystal structure of wild-type alpha-lytic protease at 1.6 a, pH 5.14 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QRX
- Type
- protein
- Length
- 198 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.6
- Source
- Lysobacter enzymogenes
- Molecule
- Alpha-lytic protease
- EC
- 3.4.21.12
- UniProt
- P00778
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.29
Structure
x-ray diffraction · resolution 1.6 · 1 distinct chain · 7% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-lytic protease (EC 3.4.21.12) | protein | 198 | 7% helix, 55% strand | P00778 |
Ligands and binding sites
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 | 53 | 0.29 | 0.75 | 17 | SO4, GOL |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1QRX · Crystal structure of wild-type alpha-lytic protease at 1.6 a, pH 5.14 · the same entry in another collection · chain A against A, TM-score 1.00
- P00778 · AlphaFold monomer V2.0 prediction for alpha-lytic protease (P00778) · a predicted model of the same protein · 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 P00778
- Elsewhere: RCSB PDB 1QRX · PDBe 1QRX · UniProt P00778
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