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Structure of the murine Fab 1G6 bound to the vaccinia virus A27 peptide 31-40
Analyse Structure of the murine Fab 1G6 bound to the vaccinia virus A27 peptide 31-40 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5EOQ
- Type
- protein
- Length
- 444 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Anti vaccinia virus A27 antibody Fab 1G6 heavy chain; Anti vaccinia virus A27 antibody…
- UniProt
- P11258
- Pockets
- 4 · best druggability 0.65
Structure
x-ray diffraction · 3 distinct chains · 6% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| H | Anti vaccinia virus A27 antibody Fab 1G6 heavy chain | protein | 217 | 7% helix, 52% strand | — |
| L | Anti vaccinia virus A27 antibody Fab 1G6 light chain | protein | 218 | 6% helix, 51% strand | — |
| A | Protein A27 | protein | 9 | 0% helix, 11% strand | P11258 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 642 | 0.65 | 0.75 | 61 | empty |
| 2 | 98 | 0.36 | 0.74 | 19 | empty |
| 3 | 94 | 0.35 | 0.74 | 26 | empty |
| 4 | 59 | 0.29 | 0.74 | 14 | empty |
Interfaces
3 interfaces between chains.
- H–L · 1769 Ų buried · 18 hydrogen bonds · protein-protein
- H–A · 371 Ų buried · 9 hydrogen bonds · protein-protein
- L–A · 367 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 5EOQ · Structure of the murine Fab 1G6 bound to the vaccinia virus A27 peptide 31-40 · 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
- Every structure of UniProt P11258
- Elsewhere: RCSB PDB 5EOQ · PDBe 5EOQ · UniProt P11258
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