Research workbench
Pro region C-terminus: protease active site interactions are critical in catalyzing the folding of alpha-lytic protease
Analyse Pro region C-terminus: protease active site interactions are critical in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BOQ
- Type
- protein
- Length
- 198 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00778
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 198 | — | P00778 |
Compared structures
- 1BOQ · Pro region C-terminus: protease active site interactions are critical in catalyzing the… · 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 1BOQ · PDBe 1BOQ · UniProt P00778
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