Research workbench
Crystal structure of the mutant S202W/I203F of the esterase E40
Analyse Crystal structure of the mutant S202W/I203F of the esterase E40 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5GMS
- Type
- protein
- Length
- 594 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Esterase
- UniProt
- A0A0F6WGE1
- Pockets
- 6 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Esterase | protein | 297 | 44% helix, 18% strand | A0A0F6WGE1 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 579 | 0.84 | 0.90 | 49 | empty |
| 2 | 326 | 0.77 | 0.88 | 54 | empty |
| 3 | 286 | 0.73 | 0.86 | 37 | empty |
| 4 | 199 | 0.48 | 0.76 | 33 | empty |
| 5 | 68 | 0.46 | 0.83 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 834 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
- 5GMS · Crystal structure of the mutant S202W/I203F of the esterase E40 · 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
- Every structure of UniProt A0A0F6WGE1
- Elsewhere: RCSB PDB 5GMS · PDBe 5GMS · UniProt A0A0F6WGE1
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