Research workbench
Structure of the extracellular portion of mouse CD200R
Analyse Structure of the extracellular portion of mouse CD200R in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BFG
- Type
- protein
- Length
- 190 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell surface glycoprotein CD200 receptor 1
- UniProt
- Q9ES57
- Ligands
- CYS, NAG, AZI
- Pockets
- 1 · best druggability 0.41
Structure
x-ray diffraction · 1 distinct chain · 2% helix, 58% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell surface glycoprotein CD200 receptor 1 | protein | 190 | 2% helix, 58% strand | Q9ES57 |
Ligands and binding sites
- CYS · Cysteine · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
- AZI · Azide ion · ion · chains A
- ACT · Acetate ion · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 104 | 0.41 | 0.76 | 21 | NAG |
Modifications
Observed in the structure: 4 disulfide, 3 glycan, 1 covalent (disulfide, N-glycosylation, covalent ligand).
Compared structures
- 4BFG · Structure of the extracellular portion of mouse CD200R · the same entry in another collection · chain A against A, TM-score 1.00
- Q9ES57 · AlphaFold monomer V2.0 prediction for cell surface glycoprotein CD200 receptor 1 (Q9ES57) · a predicted model of the same protein · chain A against A, TM-score 0.92
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 Q9ES57
- Elsewhere: RCSB PDB 4BFG · PDBe 4BFG · UniProt Q9ES57
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