Research workbench
Complex of leech-derived tryptase inhibitor with porcine trypsin
Analyse Complex of leech-derived tryptase inhibitor 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
- 1LDT
- Type
- protein
- Length
- 269 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trypsin; Tryptase inhibitor
- EC
- 3.4.21.4
- UniProt
- P00761, P80424
- Ligands
- CA
- Pockets
- 2 · best druggability 0.59
Structure
x-ray diffraction · 2 distinct chains · 11% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| T | Trypsin (EC 3.4.21.4) | protein | 223 | 10% helix, 38% strand | P00761 |
| L | Tryptase inhibitor | protein | 46 | 15% helix, 20% strand | P80424 |
Ligands and binding sites
- CA · Calcium ion · metal · chains T
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 | 237 | 0.59 | 0.79 | 31 | empty |
| 2 | 94 | 0.35 | 0.74 | 19 | empty |
Interfaces
1 interface between chains.
- T–L · 723 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 9 disulfide (disulfide).
Compared structures
- 1LDT · Complex of leech-derived tryptase inhibitor with porcine trypsin · the same entry in another collection · chain T against T, TM-score 1.00
- P00761 · AlphaFold monomer V2.0 prediction for trypsin (P00761) · a predicted model of the same protein · chain T against A, TM-score 0.99
- P80424 · AlphaFold monomer V2.0 prediction for leech-derived tryptase inhibitor C (P80424) · a predicted model of the same protein · chain L against A, TM-score 0.78
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 P80424
- Elsewhere: RCSB PDB 1LDT · PDBe 1LDT · UniProt P00761 · UniProt P80424
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