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The crystal structure of the trypsin complex with synthetic heterochiral peptide
Analyse The crystal structure of the trypsin complex with synthetic heterochiral peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1V6D
- Type
- protein
- Length
- 230 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.9
- Source
- Sus scrofa; SYNTHETIC CONSTRUCT
- Molecule
- Trypsin; PD(AIB)L(AIB)LA
- EC
- 3.4.21.4
- UniProt
- P00761
- Ligands
- TBF, NME, CA
Structure
x-ray diffraction · resolution 1.9 · 2 distinct chains · 10% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trypsin (EC 3.4.21.4) | protein | 223 | 10% helix, 35% strand | P00761 |
| B | PD(AIB)L(AIB)LA | protein | 7 | 0% helix, 0% strand | — |
Ligands and binding sites
- TBF · Tert-butyl formate · ligand · chains A, B
- NME · Methylamine · ligand · chains A, B
- CA · Calcium ion · metal · chains A
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 226 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 2 covalent, 2 modified (disulfide, covalent ligand, nonstandard).
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 P00761
- Elsewhere: RCSB PDB 1V6D · PDBe 1V6D · UniProt P00761
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