The human non-classical major histocompatibility complex molecule HLA-E. Determined by X-ray diffraction at 2.5 Å resolution. Released 29 Apr 2008.
Explore 3BZF in 3D Show helices and sheets RCSB PDB PDBe
3BZF contains 25 α-helices and 58 β-strands across 4 chains. 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 | 3-12 | 10 | 1 |
| α-helix | 20 | 1 | |
| β-strand | 21-28 | 8 | 1 |
| β-strand | 31-37 | 7 | 1 |
| β-strand | 46-47 | 2 | 1 |
| α-helix | 50-52 | 3 | |
| α-helix | 57-84 | 28 | |
| β-strand | 94-103 | 10 | 1 |
| β-strand | 109-118 | 10 | 1 |
| β-strand | 121-126 | 6 | 1 |
| β-strand | 133-135 | 3 | 1 |
| α-helix | 141-149 | 9 | |
| α-helix | 153-158 | 6 | |
| α-helix | 159-163 | 5 | |
| α-helix | 164-174 | 11 | |
| α-helix | 176-179 | 4 | |
| β-strand | 183 | 1 | 2 |
| β-strand | 186-193 | 8 | 3 |
| β-strand | 198-208 | 11 | 3 |
| β-strand | 209 | 1 | 2 |
| β-strand | 214-219 | 6 | 4 |
| β-strand | 222-223 | 2 | 4 |
| β-strand | 228-230 | 3 | 3 |
| α-helix | 231-233 | 3 | |
| β-strand | 234-235 | 2 | 3 |
| β-strand | 241-250 | 10 | 3 |
| α-helix | 254-256 | 3 | |
| β-strand | 257-262 | 6 | 4 |
| β-strand | 270-272 | 3 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-11 | 6 | 5 |
| β-strand | 21-30 | 10 | 5 |
| β-strand | 36-41 | 6 | 6 |
| β-strand | 44-45 | 2 | 6 |
| α-helix | 46 | 1 | |
| β-strand | 50-51 | 2 | 5 |
| α-helix | 52-54 | 3 | |
| β-strand | 55-56 | 2 | 5 |
| β-strand | 62-70 | 9 | 5 |
| β-strand | 78-83 | 6 | 6 |
| β-strand | 91-94 | 4 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-12 | 10 | 7 |
| α-helix | 20 | 1 | |
| β-strand | 21-28 | 8 | 7 |
| β-strand | 31-37 | 7 | 7 |
| β-strand | 46-47 | 2 | 7 |
| α-helix | 50-52 | 3 | |
| α-helix | 57-84 | 28 | |
| β-strand | 94-103 | 10 | 7 |
| β-strand | 109-118 | 10 | 7 |
| β-strand | 121-126 | 6 | 7 |
| β-strand | 133-135 | 3 | 7 |
| α-helix | 141-149 | 9 | |
| α-helix | 152-158 | 7 | |
| α-helix | 159-163 | 5 | |
| α-helix | 164-174 | 11 | |
| α-helix | 176-179 | 4 | |
| β-strand | 183 | 1 | 8 |
| α-helix | 184-185 | 2 | |
| β-strand | 186-193 | 8 | 9 |
| β-strand | 198-208 | 11 | 9 |
| β-strand | 209 | 1 | 8 |
| β-strand | 214-219 | 6 | 10 |
| β-strand | 222-223 | 2 | 10 |
| β-strand | 228-230 | 3 | 9 |
| α-helix | 231-233 | 3 | |
| β-strand | 234-235 | 2 | 9 |
| β-strand | 241-250 | 10 | 9 |
| α-helix | 254-256 | 3 | |
| β-strand | 257-262 | 6 | 10 |
| β-strand | 270-272 | 3 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-11 | 6 | 11 |
| β-strand | 21-22 | 2 | 12 |
| β-strand | 23-30 | 8 | 11 |
| β-strand | 36-41 | 6 | 13 |
| β-strand | 44-45 | 2 | 13 |
| α-helix | 46 | 1 | |
| β-strand | 50-51 | 2 | 11 |
| α-helix | 52-54 | 3 | |
| β-strand | 55-56 | 2 | 11 |
| β-strand | 62-67 | 6 | 11 |
| β-strand | 69-70 | 2 | 12 |
| β-strand | 78-83 | 6 | 13 |
| β-strand | 91-94 | 4 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| HLA class I histocompatibility antigen, alpha chain E | A, C | protein | 276 | Homo sapiens | P13747 (AlphaFold model) |
| Beta-2-microglobulin | B, D | protein | 97 | Homo sapiens | P61769 (AlphaFold model) |
| leader peptide of HLA class I histocompatibility antigen, Cw-7 alpha chain | P, Q | protein | 9 | P10321 (AlphaFold model) |
>3BZF_1 HLA class I histocompatibility antigen, alpha chain E (chains A, C) GSHSLKYFHTSVSRPGRGEPRFISVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYW DRETRSARDTAQIFRVNLRTLRGYYNQSEAGSHTLQWMHGCELGPDRRFLRGYEQFAYDG KDYLTLNEDLRSWTAVDTAAQISEQKSNDASEAEHQRAYLEDTCVEWLHKYLEKGKETLL HLEPPKTHVTHHPISDHEATLRCWALGFYPAEITLTWQQDGEGHTQDTELVETRPAGDGT FQKWAAVVVPSGEEQRYTCHVQHEGLPEPVTLRWKP
>3BZF_2 Beta-2-microglobulin (chains B, D) RTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSF YLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
>3BZF_3 leader peptide of HLA class I histocompatibility antigen, Cw-7 alpha chain (chains P, Q) VMAPRALLL
Subtle changes in peptide conformation profoundly affect recognition of the non-classical MHC class I molecule HLA-E by the CD94-NKG2 natural killer cell receptors. Hoare, H.L., Sullivan, L.C., Clements, C.S. et al. J Mol Biol (2008) 377:1297-1303. DOI 10.1016/j.jmb.2008.01.098 · PubMed
Other PDB entries of the same protein (UniProt P13747 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 3BZF directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.