MolNFT v1 · #23157 · protein
The three-dimensional structure of ASN102 mutant of trypsin. role of ASP102 in serine protease catalysis
1TRM: “The three-dimensional structure of ASN102 mutant of trypsin. role of ASP102 in serine protease catalysis”. X-ray diffraction, 2 ligands (BEN, CA), 3 pockets (best druggability 0.39). MolNFT v1 #23157 on GenesisL1: 3D structure…
- PDB
- 1TRM
- Type
- protein
- Length
- 446 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trypsin
- EC
- 3.4.21.4
- UniProt
- P00763
- Ligands
- BEN, CA
- Pockets
- 3 · best druggability 0.39
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Trypsin (EC 3.4.21.4) | protein | 223 | 10% helix, 35% strand | P00763 |
Ligands and binding sites
- BEN · Benzamidine · ligand · 2 copies · chains A, B
- CA · Calcium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 128 | 0.39 | 0.74 | 21 | empty |
| 2 | 53 | 0.37 | 0.81 | 17 | BEN |
| 3 | 64 | 0.28 | 0.74 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 205 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 disulfide (disulfide).
Compared structures
- 1TRM · The three-dimensional structure of ASN102 mutant of trypsin. role of ASP102 in serine… · the same entry in another collection · chain A against A, TM-score 1.00
- P00763 · AlphaFold monomer V2.0 prediction for anionic trypsin-2 (P00763) · a predicted model of the same protein · 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 P00763
- Elsewhere: RCSB PDB 1TRM · PDBe 1TRM · UniProt P00763
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