Research workbench
Kunitz type trypsin inhibitor complex with porcine trypsin
Analyse Kunitz type trypsin inhibitor complex with porcine trypsin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AN7
- Type
- protein
- Length
- 379 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trypsin; Trypsin inhibitor
- EC
- 3.4.21.4
- UniProt
- P00761, F4ZZG4
- Ligands
- CA
- Pockets
- 2 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trypsin (EC 3.4.21.4) | protein | 223 | 10% helix, 36% strand | P00761 |
| B | Trypsin inhibitor | protein | 156 | 0% helix, 42% strand | F4ZZG4 |
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.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 367 | 0.62 | 0.78 | 58 | empty |
| 2 | 126 | 0.41 | 0.75 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 954 Ų buried · 23 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
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
- Every structure of UniProt F4ZZG4
- Elsewhere: RCSB PDB 4AN7 · PDBe 4AN7 · UniProt P00761 · UniProt F4ZZG4
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