Research workbench
Structural basis for a germline-biased antibody response to SARS-cov-2 (RBD:C1A-B12 Fab)
Analyse Structural basis for a germline-biased antibody response to SARS-cov-2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7KFV
- Type
- protein
- Length
- 1,896 residues
- Chains
- 9
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0DTC2
- Ligands
- NAG
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, E | — | protein | 195 | — | P0DTC2 |
| C, H | — | protein | 225 | — | — |
| D, G, L | — | protein | 214 | — | — |
| F | — | protein | 219 | — | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A, B, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7KFV · Structural basis for a germline-biased antibody response to SARS-CoV-2 (RBD:C1A-B12 Fab) · 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 P0DTC2
- Elsewhere: RCSB PDB 7KFV · PDBe 7KFV · UniProt P0DTC2
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