Research workbench
Crystal structure and binding properties of the CD2 and CD244 (2B4) binding protein, CD48
Analyse Crystal structure and binding properties of the CD2 and CD244 (2B4) binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2DRU
- Type
- protein
- Length
- 180 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chimera of CD48 antigen and T-cell surface antigen CD2
- UniProt
- P10252
- Ligands
- NAG
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chimera of CD48 antigen and T-cell surface antigen CD2 | protein | 180 | 3% helix, 48% strand | P10252 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
- GOL · Glycerol · additive · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 glycan, 2 disulfide (N-glycosylation, disulfide).
Compared structures
- 2DRU · Crystal structure and binding properties of the CD2 and CD244 (2B4) binding protein, CD48 · the same entry in another collection · chain A against A, TM-score 1.00
- P10252 · AlphaFold monomer V2.0 prediction for CD48 antigen (P10252) · a predicted model of the same protein · chain A against A, TM-score 0.88
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 P10252
- Elsewhere: RCSB PDB 2DRU · PDBe 2DRU · UniProt P10252
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