Research workbench
Trypsin specificity as elucidated by LIE calculations, X-ray structures and association constant measurements
Analyse Trypsin specificity as elucidated by LIE calculations, X-ray structures and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UTO
- Type
- protein
- Length
- 223 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.15
- Source
- BOS TAURUS
- Molecule
- Trypsinogen
- EC
- 3.4.21.4
- UniProt
- P00760
- Ligands
- PEA, CA
Structure
x-ray diffraction · resolution 1.15 · 1 distinct chain · 10% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trypsinogen (EC 3.4.21.4) | protein | 223 | 10% helix, 35% strand | P00760 |
Ligands and binding sites
- PEA · 2-phenylethylamine · ligand · chains A
- CA · Calcium ion · metal · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 1UTO · Trypsin specificity as elucidated by lie calculations, X-ray structures and association… · the same entry in another collection · 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 P00760
- Elsewhere: RCSB PDB 1UTO · PDBe 1UTO · UniProt P00760
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