N-glycan and polypeptide NMR solution structures of the adhesion domain of human CD2. Determined by solution NMR. Released 8 Nov 1996.
Explore 1GYA in 3D Show helices and sheets RCSB PDB PDBe
1GYA contains 0 α-helices and 11 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-9 | 3 | 1 |
| β-strand | 17 | 1 | 2 |
| β-strand | 30-37 | 8 | 1 |
| β-strand | 42-48 | 7 | 1 |
| β-strand | 50 | 1 | 1 |
| β-strand | 54 | 1 | 1 |
| β-strand | 61-62 | 2 | 3 |
| β-strand | 68-69 | 2 | 3 |
| β-strand | 70 | 1 | 2 |
| β-strand | 80-87 | 8 | 1 |
| β-strand | 95-100 | 6 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Human CD2 | A | protein | 105 | Homo sapiens | P06729 (AlphaFold model) |
>1GYA_1 HUMAN CD2 (chains A) KEITNALETWGALGQDINLDIPSFQMSDDIDDIKWEKTSDKKKIAQFRKEKETFKEKDTY KLFKNGTLKIKHLKTDDQDIYKVSIYDTKGKNVLEKIFDLKIQER
Conformation and function of the N-linked glycan in the adhesion domain of human CD2. Wyss, D.F., Choi, J.S., Li, J. et al. Science (1995) 269:1273-1278. PubMed
Other PDB entries of the same protein (UniProt P06729 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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