Research workbench
Crystal structure of esterase E22 L374D mutant
Analyse Crystal structure of esterase E22 L374D mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5JKJ
- Type
- protein
- Length
- 739 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Esterase E22
- Pockets
- 9 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Esterase E22 | protein | 370 | 42% helix, 17% strand | — |
| B | Esterase E22 | protein | 369 | 39% helix, 17% strand | — |
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 556 | 0.77 | 0.84 | 57 | empty |
| 2 | 409 | 0.65 | 0.79 | 40 | empty |
| 3 | 192 | 0.57 | 0.80 | 22 | empty |
| 4 | 202 | 0.57 | 0.80 | 27 | empty |
| 5 | 69 | 0.40 | 0.79 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 2663 Ų buried · 45 hydrogen bonds · protein-protein
Compared structures
- 5JKJ · Crystal structure of esterase E22 L374D mutant · the same entry in another collection · 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
- Elsewhere: RCSB PDB 5JKJ · PDBe 5JKJ
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