Human CD94. Determined by X-ray diffraction at 2.6 Å resolution. Released 15 Jun 1999.
Explore 1B6E in 3D Show helices and sheets RCSB PDB PDBe
1B6E contains 5 α-helices and 12 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 | 66-68 | 3 | 1 |
| β-strand | 71-75 | 5 | 1 |
| β-strand | 80 | 1 | 2 |
| α-helix | 82-91 | 10 | |
| β-strand | 96 | 1 | 1 |
| β-strand | 115-122 | 8 | 3 |
| α-helix | 123-125 | 3 | |
| β-strand | 127-129 | 3 | 3 |
| α-helix | 134 | 1 | |
| β-strand | 135 | 1 | 3 |
| α-helix | 136-137 | 2 | |
| α-helix | 144-146 | 3 | |
| β-strand | 151-155 | 5 | 3 |
| β-strand | 161-165 | 5 | 3 |
| β-strand | 170 | 1 | 2 |
| β-strand | 171-172 | 2 | 3 |
| β-strand | 173-176 | 4 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| CD94 | A | protein | 128 | Homo sapiens | Q13241 (AlphaFold model) |
>1B6E_1 CD94 (chains A) LQKDSDCCSCQEKWVGYRCNCYFISSEQKTWNESRHLCASQKSSLLQLQNTDELDFMSSS QQFYWIGLSYSEEHTAWLWENGSALSQYLFPSFETFNTKNCIAYNPNGNALDESCEDKNR YICKQQLI
Structure of CD94 reveals a novel C-type lectin fold: implications for the NK cell-associated CD94/NKG2 receptors. Boyington, J.C., Riaz, A.N., Patamawenu, A. et al. Immunity (1999) 10:75-82. DOI 10.1016/S1074-7613(00)80008-4 · PubMed
Other PDB entries of the same protein (UniProt Q13241 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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