Research workbench
Single chain fv of C219 heavy chain V101L mutant in complex with synthetic epitope peptide
Analyse Single chain fv of C219 heavy chain V101L mutant in complex with synthetic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MVU
- Type
- protein
- Length
- 246 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ig kappa-chain vj-region (light chain); Ig vdj-region (heavy chain); P-glycoprotein
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.30
Structure
x-ray diffraction · 3 distinct chains · 9% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ig kappa-chain vj-region (light chain) | protein | 112 | 3% helix, 49% strand | — |
| B | Ig vdj-region (heavy chain) | protein | 121 | 7% helix, 50% strand | — |
| P | P-glycoprotein | protein | 13 | 77% helix, 0% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 64 | 0.30 | 0.74 | 15 | empty |
| 2 | 66 | 0.28 | 0.73 | 21 | empty |
| 3 | 61 | 0.27 | 0.73 | 11 | empty |
Interfaces
3 interfaces between chains.
- A–B · 883 Ų buried · 11 hydrogen bonds · protein-protein
- B–P · 336 Ų buried · 5 hydrogen bonds · protein-protein
- A–P · 254 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1MVU · Single chain fv of C219 heavy chain V101L mutant in complex with synthetic epitope peptide · the same entry in another collection · chain A against A, 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 1MVU · PDBe 1MVU
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