Research workbench
Crystal structure of human trypsin 1: unexpected phosphorylation of tyrosine 151
Analyse Crystal structure of human trypsin 1: unexpected phosphorylation of tyrosine 151 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TRN
- Type
- protein
- Length
- 448 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trypsin
- EC
- 3.4.21.4
- UniProt
- P07477
- Ligands
- ISP
- Pockets
- 6 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Trypsin (EC 3.4.21.4) | protein | 224 | 11% helix, 36% strand | P07477 |
Ligands and binding sites
- ISP · Phosphorylisopropane · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 53 | 0.58 | 0.91 | 15 | empty |
| 2 | 227 | 0.51 | 0.75 | 36 | empty |
| 3 | 88 | 0.49 | 0.83 | 19 | empty |
| 4 | 66 | 0.49 | 0.85 | 15 | empty |
| 5 | 73 | 0.35 | 0.77 | 21 | ISP |
Interfaces
1 interface between chains.
- A–B · 274 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide, 2 covalent, 2 modified (disulfide, covalent ligand, phosphorylation).
Compared structures
- 1TRN · Crystal structure of human trypsin 1: unexpected phosphorylation of tyrosine 151 · the same entry in another collection · chain B against B, TM-score 1.00
- P07477 · AlphaFold monomer V2.0 prediction for trypsin-1 (P07477) · 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 P07477
- Elsewhere: RCSB PDB 1TRN · PDBe 1TRN · UniProt P07477
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.