Research workbench
Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 ångströms resolution
Analyse Crystal structure of the extracellular region of the human cell adhesion… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HNF
- Type
- protein
- Length
- 179 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CD2
- UniProt
- P06729
- Ligands
- NAG, NA
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CD2 | protein | 179 | 5% helix, 54% strand | P06729 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
- NA · Sodium ion · metal · 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
- 1HNF · Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at… · the same entry in another collection · chain A against A, TM-score 1.00
- P06729 · AlphaFold monomer V2.0 prediction for T-cell surface antigen CD2 (P06729) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P06729
- Elsewhere: RCSB PDB 1HNF · PDBe 1HNF · UniProt P06729
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