Research workbench
MERS-cov S bound to the broadly neutralizing B6 Fab fragment (C3 refinement)
Analyse MERS-cov S bound to the broadly neutralizing B6 Fab fragment (C3 refinement) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7M5E
- Type
- protein
- Length
- 3,480 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A140AYW5
- Ligands
- NAG, MAN, BMA, SIA
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E | — | protein | 1160 | — | A0A140AYW5 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 81 copies · chains A, C, E
- MAN · alpha-D-mannopyranose · sugar · 30 copies · chains A, C, E
- BMA · beta-D-mannopyranose · sugar · 18 copies · chains A, C, E
- SIA · N-acetyl-alpha-neuraminic acid · sugar · 3 copies · chains A, C, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7M5E · MERS-CoV S bound to the broadly neutralizing B6 Fab fragment (C3 refinement) · 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 A0A140AYW5
- Elsewhere: RCSB PDB 7M5E · PDBe 7M5E · UniProt A0A140AYW5
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