Research workbench
L29I mutation in an aryl esterase from pseudomonas fluorescens leads to unique peptide flip and increased activity
Analyse L29I mutation in an aryl esterase from pseudomonas fluorescens leads to unique… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3T52
- Type
- protein
- Length
- 1,626 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arylesterase
- EC
- 3.1.1.2, 1.-.-.-
- UniProt
- P22862
- Ligands
- PEO, SO4, CL
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Arylesterase (EC 3.1.1.2, 1.-.-.-) | protein | 271 | 47% helix, 18% strand | P22862 |
Ligands and binding sites
- PEO · Hydrogen peroxide · ligand · 19 copies · chains A, B, C, D, E, F
- SO4 · Sulfate ion · ion · 12 copies · chains A, B, C, D, E, F
- CL · Chloride ion · ion · 7 copies · chains A, B, C, D, E
- GOL · Glycerol · additive · 32 copies · chains A, C, B, D, E, F
- ACT · Acetate ion · additive · 28 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 594 | 0.78 | 0.84 | 47 | PEO |
| 2 | 570 | 0.77 | 0.84 | 48 | empty |
| 3 | 172 | 0.68 | 0.87 | 35 | empty |
| 4 | 145 | 0.67 | 0.88 | 34 | GOL |
| 5 | 145 | 0.66 | 0.87 | 34 | PEO |
Interfaces
7 interfaces between chains.
- A–C · 813 Ų buried · 11 hydrogen bonds · protein-protein
- D–E · 813 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 810 Ų buried · 9 hydrogen bonds · protein-protein
- D–F · 804 Ų buried · 8 hydrogen bonds · protein-protein
- E–F · 803 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 3T52 · L29I Mutation in an Aryl Esterase from Pseudomonas fluorescens Leads to Unique Peptide… · the same entry in another collection · chain F against F, TM-score 1.00
- P22862 · AlphaFold monomer V2.0 prediction for arylesterase (P22862) · a predicted model of the same protein · chain D 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 P22862
- Elsewhere: RCSB PDB 3T52 · PDBe 3T52 · UniProt P22862
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