Research workbench
Human beta-1 tryptase mutant ILE99CYS
Analyse Human beta-1 tryptase mutant ILE99CYS in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WI6
- Type
- protein
- Length
- 972 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tryptase ALPHA/BETA-1
- EC
- 3.4.21.59
- UniProt
- Q15661
- Ligands
- 0GJ, SO4
- Pockets
- 12 · best druggability 0.54
Structure
x-ray diffraction · 3 distinct chains · 11% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Tryptase ALPHA/BETA-1 (EC 3.4.21.59) | protein | 243 | 11% helix, 37% strand | Q15661 |
| B | Tryptase ALPHA/BETA-1 (EC 3.4.21.59) | protein | 244 | 11% helix, 36% strand | Q15661 |
| C | Tryptase ALPHA/BETA-1 (EC 3.4.21.59) | protein | 242 | 11% helix, 38% strand | Q15661 |
Ligands and binding sites
- 0GJ · L-alpha-glutamyl-N-{(1S)-4-{[amino(iminio)methyl]amino}-1-[(1S)-2-chloro-1-hydroxyethyl]butyl}glycinamide · ligand · 4 copies · chains A, B, C, D
- SO4 · Sulfate ion · ion · 7 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 260 | 0.54 | 0.76 | 33 | empty |
| 2 | 272 | 0.53 | 0.75 | 35 | empty |
| 3 | 206 | 0.52 | 0.77 | 35 | empty |
| 4 | 78 | 0.44 | 0.81 | 19 | 0GJ |
| 5 | 88 | 0.42 | 0.79 | 20 | empty |
Interfaces
4 interfaces between chains.
- B–C · 1116 Ų buried · 15 hydrogen bonds · protein-protein
- A–D · 1107 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 481 Ų buried · 1 hydrogen bond · protein-protein
- A–B · 479 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 18 disulfide, 8 covalent (disulfide, covalent ligand).
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 Q15661
- Elsewhere: RCSB PDB 5WI6 · PDBe 5WI6 · UniProt Q15661
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