MolNFT v1 · #14912 · protein
The three-dimensional structure of an engineered scfv T84.66 dimer or diabody in vl to vh linkage.
1MOE · Anti-cea mab T84.66: “The three-dimensional structure of an engineered scfv T84.66 dimer or diabody in vl to vh linkage.”. X-ray diffraction, 1 ligand (SO4), 5 pockets (best druggability 0.65). MolNFT v1 #14912 on GenesisL1: 3D…
- PDB
- 1MOE
- Type
- protein
- Length
- 480 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Anti-cea mab T84.66
- UniProt
- P01660
- Ligands
- SO4
- Pockets
- 5 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Anti-cea mab T84.66 | protein | 240 | 5% helix, 47% strand | P01660 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 577 | 0.65 | 0.76 | 63 | SO4 |
| 2 | 193 | 0.46 | 0.75 | 40 | empty |
| 3 | 87 | 0.34 | 0.74 | 16 | empty |
| 4 | 81 | 0.33 | 0.74 | 22 | empty |
| 5 | 87 | 0.30 | 0.72 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 1839 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1MOE · The three-dimensional structure of an engineered scFv T84.66 dimer or diabody in VL to VH… · the same entry in another collection · chain A against A, TM-score 1.00
- P01660 · AlphaFold monomer V2.0 prediction for ig kappa chain V-III region pc 3741/TEPC 111… · a predicted model of the same protein · chain A against A, TM-score 0.46
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 P01660
- Elsewhere: RCSB PDB 1MOE · PDBe 1MOE · UniProt P01660
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