Research workbench
Pseudomonas fluorescens esterase complexed to the R-enantiomer of a sulfonate transition state analog
Analyse Pseudomonas fluorescens esterase complexed to the R-enantiomer of a sulfonate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3IA2
- 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
- J6Z, SO4
- Pockets
- 20 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 46% 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 | 46% helix, 18% strand | P22862 |
Ligands and binding sites
- J6Z · (2R)-butane-2-sulfonate · ligand · 6 copies · chains A, B, C, D, E, F
- SO4 · Sulfate ion · ion · 5 copies · chains A, B, C, D, E
- GOL · Glycerol · additive · 25 copies · chains A, C, B, 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, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 600 | 0.79 | 0.85 | 48 | empty |
| 2 | 584 | 0.78 | 0.84 | 47 | empty |
| 3 | 125 | 0.69 | 0.90 | 28 | GOL |
| 4 | 167 | 0.68 | 0.87 | 33 | GOL |
| 5 | 115 | 0.68 | 0.90 | 26 | GOL |
Interfaces
7 interfaces between chains.
- A–C · 813 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 812 Ų buried · 9 hydrogen bonds · protein-protein
- E–F · 808 Ų buried · 9 hydrogen bonds · protein-protein
- D–F · 805 Ų buried · 10 hydrogen bonds · protein-protein
- D–E · 803 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 covalent (covalent ligand).
Compared structures
- 3IA2 · Pseudomonas fluorescens esterase complexed to the R-enantiomer of a sulfonate transition… · 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 C 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 3IA2 · PDBe 3IA2 · UniProt P22862
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