Research workbench
Crystal structure of a chimeric MR78-like antibody chimera-1 Fab
Analyse Crystal structure of a chimeric MR78-like antibody chimera-1 Fab in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6V4R
- Type
- protein
- Length
- 430 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chimera-1 Fab heavy chain; Chimera-1 Fab light chain
- Pockets
- 3 · best druggability 0.59
Structure
x-ray diffraction · 2 distinct chains · 5% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| H | Chimera-1 Fab heavy chain | protein | 220 | 5% helix, 55% strand | — |
| L | Chimera-1 Fab light chain | protein | 210 | 6% helix, 53% strand | — |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 527 | 0.59 | 0.74 | 59 | empty |
| 2 | 185 | 0.45 | 0.74 | 31 | empty |
| 3 | 81 | 0.33 | 0.75 | 23 | empty |
Interfaces
1 interface between chains.
- H–L · 1935 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 6V4R · Crystal structure of a chimeric MR78-like antibody chimera-1 Fab · the same entry in another collection · chain H against H, 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 6V4R · PDBe 6V4R
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