Research workbench
Crystal structure of quorum-quenching antibody 1G9
Analyse Crystal structure of quorum-quenching antibody 1G9 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OP4
- Type
- protein
- Length
- 429 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Murine antibody Fab RS2-1G9 lambda light chain; Murine antibody Fab RS2-1G9 IGG1 heavy…
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | Murine antibody Fab RS2-1G9 lambda light chain | protein | 212 | 7% helix, 55% strand | — |
| H | Murine antibody Fab RS2-1G9 IGG1 heavy chain | protein | 217 | 6% helix, 51% strand | — |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · chains L, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 635 | 0.69 | 0.78 | 56 | empty |
| 2 | 128 | 0.40 | 0.74 | 23 | empty |
| 3 | 58 | 0.30 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- L–H · 2031 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 2OP4 · Crystal Structure of Quorum-Quenching Antibody 1G9 · 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 2OP4 · PDBe 2OP4
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