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Crystal structure of monoclonal human anti-rhesus D Fc IGG1 T125(YB2/0) double mutant (H310 and H435 in K)
Analyse Crystal structure of monoclonal human anti-rhesus D Fc IGG1 T125(YB2/0) double… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3V8C
- Type
- protein
- Length
- 421 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ig gamma-1 chain C region
- UniProt
- P01857
- Ligands
- NAG, MAN, GAL
- Pockets
- 2 · best druggability 0.48
Structure
x-ray diffraction · 2 distinct chains · 9% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ig gamma-1 chain C region | protein | 212 | 9% helix, 47% strand | P01857 |
| B | Ig gamma-1 chain C region | protein | 209 | 10% helix, 37% strand | P01857 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, B
- MAN · alpha-D-mannopyranose · sugar · 6 copies · chains B, A
- GAL · beta-D-galactopyranose · sugar · 2 copies · chains A, B
- GOL · Glycerol · additive · 3 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 218 | 0.48 | 0.74 | 33 | empty |
| 2 | 53 | 0.28 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1134 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 3V8C · Crystal structure of monoclonal human anti-rhesus D Fc IgG1 t125(yb2/0) double mutant… · 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
- Every structure of UniProt P01857
- Elsewhere: RCSB PDB 3V8C · PDBe 3V8C · UniProt P01857
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