Research workbench
Pro region of alpha-lytic protease
Analyse Pro region of alpha-lytic protease in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2PRO
- Type
- protein
- Length
- 414 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-lytic protease
- UniProt
- P00778
- Pockets
- 3 · best druggability 0.32
Structure
x-ray diffraction · 3 distinct chains · 40% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-lytic protease | protein | 142 | 43% helix, 21% strand | P00778 |
| B | Alpha-lytic protease | protein | 143 | 38% helix, 22% strand | P00778 |
| C | Alpha-lytic protease | protein | 129 | 38% helix, 20% strand | P00778 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 76 | 0.32 | 0.74 | 16 | empty |
| 2 | 68 | 0.30 | 0.74 | 13 | empty |
| 3 | 57 | 0.25 | 0.72 | 11 | empty |
Interfaces
2 interfaces between chains.
- A–B · 608 Ų buried · 16 hydrogen bonds · protein-protein
- B–C · 598 Ų buried · 10 hydrogen bonds · protein-protein
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 2PRO · PDBe 2PRO · UniProt P00778
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