Research workbench
Crystal structure of alpha-lytic protease SB1+2 R64A/E182Q mutant
Analyse Crystal structure of alpha-lytic protease SB1+2 R64A/E182Q mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3M7U
- Type
- protein
- Length
- 202 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-lytic protease; Self-proteolysis product (residues 184-187)
- EC
- 3.4.21.12
- UniProt
- P00778
- Ligands
- SO4
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 54% 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 |
| B | Self-proteolysis product (residues 184-187) | protein | 4 | 0% helix, 0% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · 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 · 337 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
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 3M7U · PDBe 3M7U · UniProt P00778
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