Research workbench
Structural basis for broad specificity in alpha-lytic protease mutants
Analyse Structural basis for broad specificity in alpha-lytic protease mutants in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3LPR
- Type
- protein
- Length
- 201 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-lytic protease; Methoxysuccinyl-ala-ala-pro-norleucine boronic acid inhibitor
- EC
- 3.4.21.12
- UniProt
- P00778
- Ligands
- BNO, SO4
Structure
x-ray diffraction · 2 distinct chains · 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 |
| P | Methoxysuccinyl-ala-ala-pro-norleucine boronic acid inhibitor | protein | 3 | 0% helix, 33% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–P · 243 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide, 2 covalent (disulfide, covalent ligand).
Compared structures
- 3LPR · Structural basis for broad specificity in alpha-lytic protease mutants · 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 3LPR · PDBe 3LPR · UniProt P00778
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