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Crystal structure of human monoclonal antibody HEPC46
Analyse Crystal structure of human monoclonal antibody HEPC46 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MEG
- Type
- protein
- Length
- 432 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Antibody HEPC46 heavy chain; Antibody HEPC46 light chain
- Pockets
- 4 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 9% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| H | Antibody HEPC46 heavy chain | protein | 219 | 11% helix, 52% strand | — |
| L | Antibody HEPC46 light chain | protein | 213 | 7% helix, 50% strand | — |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 394 | 0.57 | 0.74 | 52 | empty |
| 2 | 134 | 0.53 | 0.81 | 20 | empty |
| 3 | 110 | 0.46 | 0.80 | 26 | empty |
| 4 | 65 | 0.33 | 0.76 | 19 | empty |
Interfaces
1 interface between chains.
- H–L · 1770 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 6MEG · Crystal structure of human monoclonal antibody HEPC46 · 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 6MEG · PDBe 6MEG
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