Research workbench
Structure of the extracellular portion of mouse CD200RLA
Analyse Structure of the extracellular portion of mouse CD200RLA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BFE
- Type
- protein
- Length
- 563 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell surface glycoprotein CD200 receptor 4
- UniProt
- Q6XJV4
- Ligands
- CYS, NAG, SO4
Structure
x-ray diffraction · 2 distinct chains · 2% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cell surface glycoprotein CD200 receptor 4 | protein | 188 | 2% helix, 56% strand | Q6XJV4 |
| C | Cell surface glycoprotein CD200 receptor 4 | protein | 187 | 2% helix, 57% strand | Q6XJV4 |
Ligands and binding sites
- CYS · Cysteine · ligand · 3 copies · chains A, B, C
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 15 copies · chains A, B, C
- SO4 · Sulfate ion · ion · 7 copies · chains A, B, C
- GOL · Glycerol · additive · 3 copies · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–B · 636 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 633 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 631 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 15 glycan, 12 disulfide, 3 covalent (N-glycosylation, disulfide, covalent ligand).
Compared structures
- 4BFE · Structure of the extracellular portion of mouse CD200RLa · the same entry in another collection · chain C against C, TM-score 1.00
- Q6XJV4 · AlphaFold monomer V2.0 prediction for cell surface glycoprotein CD200 receptor 4 (Q6XJV4) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q6XJV4
- Elsewhere: RCSB PDB 4BFE · PDBe 4BFE · UniProt Q6XJV4
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