Research workbench
Complex of SARS-cov-2 receptor binding domain with the Fab fragments of neutralizing antibodies REGN10985 and REGN10989
Analyse Complex of SARS-cov-2 receptor binding domain with the Fab fragments of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7M42
- Type
- protein
- Length
- 1,070 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0DTC2
- Ligands
- NAG, BMA
Structure
electron microscopy · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 210 | — | — |
| B | — | protein | 224 | — | — |
| E | — | protein | 195 | — | P0DTC2 |
| C | — | protein | 213 | — | — |
| D | — | protein | 228 | — | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains E
- BMA · beta-D-mannopyranose · sugar
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7M42 · Complex of SARS-CoV-2 receptor binding domain with the Fab fragments of neutralizing… · 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 7M42 · PDBe 7M42 · UniProt P0DTC2
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