Research workbench
Crystal structure of the Fab fragment of esterolytic antibody MS5-393
Analyse Crystal structure of the Fab fragment of esterolytic antibody MS5-393 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MIE
- Type
- protein
- Length
- 409 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Immunoglobulin MS5-393
- Pockets
- 3 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | Immunoglobulin MS5-393 | protein | 218 | 6% helix, 50% strand | — |
| H | Immunoglobulin MS5-393 | protein | 191 | 7% helix, 46% strand | — |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 688 | 0.68 | 0.76 | 67 | empty |
| 2 | 157 | 0.54 | 0.80 | 21 | empty |
| 3 | 64 | 0.29 | 0.74 | 19 | empty |
Interfaces
1 interface between chains.
- L–H · 1633 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1MIE · Crystal Structure Of The Fab Fragment of Esterolytic Antibody MS5-393 · the same entry in another collection · chain L against L, 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 1MIE · PDBe 1MIE
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.