MolNFT v1 · #79500 · protein
L29I mutation in an aryl esterase from pseudomonas fluorescens leads to unique peptide flip and increased activity
3T52 · Arylesterase: “L29I mutation in an aryl esterase from pseudomonas fluorescens leads to unique peptide flip and increased…”. X-ray diffraction, 3 ligands (PEO, SO4, CL), 20 pockets (best druggability 0.78). MolNFT v1 #79500 on…
- 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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