Research workbench
Crystal structure of the bovine trypsin complex with a synthetic 11 peptide inhibitor
Analyse Crystal structure of the bovine trypsin complex with a synthetic 11 peptide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OX1
- Type
- protein
- Length
- 233 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trypsinogen, cationic; 11-mer peptide
- EC
- 3.4.21.4
- UniProt
- P00760
- Ligands
- CA
Structure
x-ray diffraction · 2 distinct chains · 9% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trypsinogen, cationic (EC 3.4.21.4) | protein | 223 | 10% helix, 35% strand | P00760 |
| B | 11-mer peptide | protein | 10 | 0% helix, 20% strand | — |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 585 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 disulfide (disulfide).
Compared structures
- 1OX1 · crystal structure of the bovine trypsin complex with a synthetic 11 peptide inhibitor · 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 1OX1 · PDBe 1OX1 · UniProt P00760
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