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
- 1UTK
- 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
- CA, SO4
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trypsin I (EC 3.4.21.4) | protein | 222 | 10% helix, 36% 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
- 1UTK · 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 0.99
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 1UTK · PDBe 1UTK · UniProt P35031
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