Research workbench
Structure of the mus musclus langerin carbohydrate recognition domain in complex with glucose
Analyse Structure of the mus musclus langerin carbohydrate recognition domain in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5M62
- Type
- protein
- Length
- 272 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q8VBX4
- Ligands
- BGC, GLC, CA
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 136 | — | Q8VBX4 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · 2 copies · chains A, B
- GLC · alpha-D-glucopyranose · sugar · chains B
- CA · Calcium ion · metal · 2 copies · chains A, B
- GOL · Glycerol · additive · 8 copies · chains A, B
- P6G · Hexaethylene glycol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5M62 · Structure of the Mus musclus Langerin carbohydrate recognition domain in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- Q8VBX4 · AlphaFold monomer V2.0 prediction for C-type lectin domain family 4 member K (Q8VBX4) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q8VBX4
- Elsewhere: RCSB PDB 5M62 · PDBe 5M62 · UniProt Q8VBX4
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