Research workbench
Crystal structure of an alpha-lytic protease mutant with accelerated folding kinetics, R102H/G134S, pH 8
Analyse Crystal structure of an alpha-lytic protease mutant with accelerated folding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QRW
- Type
- protein
- Length
- 198 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alhpa-lytic protease
- EC
- 3.4.21.12
- UniProt
- P00778
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.29
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alhpa-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 | 54 | 0.29 | 0.75 | 18 | SO4, GOL |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1QRW · Crystal structure of an alpha-lytic protease mutant with accelerated folding kinetics… · 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 1QRW · PDBe 1QRW · UniProt P00778
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