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
- 1UTJ
- Type
- protein
- Length
- 222 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trypsin I
- EC
- 3.4.21.4
- UniProt
- P35031
- Ligands
- ABN, CA
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trypsin I (EC 3.4.21.4) | protein | 222 | 10% helix, 35% strand | P35031 |
Ligands and binding sites
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
- 1UTJ · 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
- P35031 · AlphaFold monomer V2.0 prediction for trypsin-1 (P35031) · 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 P35031
- Elsewhere: RCSB PDB 1UTJ · PDBe 1UTJ · UniProt P35031
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.