Structural tuning of CD81LEL (space group P31). Determined by X-ray diffraction at 2.38 Å resolution. Released 14 Dec 2016.
Explore 5M3D in 3D Show helices and sheets RCSB PDB PDBe
5M3D contains 29 α-helices and 0 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 |
|---|---|---|---|
| α-helix | 116-136 | 21 | |
| α-helix | 141-154 | 14 | |
| α-helix | 161-170 | 10 | |
| α-helix | 172-174 | 3 | |
| α-helix | 176 | 1 | |
| α-helix | 181-185 | 5 | |
| α-helix | 188-189 | 2 | |
| α-helix | 190-199 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 116-136 | 21 | |
| α-helix | 141-154 | 14 | |
| α-helix | 161-170 | 10 | |
| α-helix | 172-174 | 3 | |
| α-helix | 176 | 1 | |
| α-helix | 183-186 | 4 | |
| α-helix | 190-199 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 116-134 | 19 | |
| α-helix | 143-154 | 12 | |
| α-helix | 161-170 | 10 | |
| α-helix | 172-174 | 3 | |
| α-helix | 182-185 | 4 | |
| α-helix | 190-199 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 116-135 | 20 | |
| α-helix | 143-154 | 12 | |
| α-helix | 161-170 | 10 | |
| α-helix | 172-174 | 3 | |
| α-helix | 176 | 1 | |
| α-helix | 182-185 | 4 | |
| α-helix | 188-189 | 2 | |
| α-helix | 190-199 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| CD81 antigen | A, B, C, D | protein | 101 | Homo sapiens | P60033 (AlphaFold model) |
>5M3D_1 CD81 antigen (chains A, B, C, D) ETGFVNKDQIAKDVKQFYDQALQQAVVDDDANNAKAVVKTFHETLDCCGSSTLTALTTSV LKNNLCPSGSNIISNLFKEDCHQKIDDLFSGKGTKHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| PO4 | Phosphate ion | O4 P | 6 |
Water and common crystallization additives (EDO) are not listed.
Mechanism of Structural Tuning of the Hepatitis C Virus Human Cellular Receptor CD81 Large Extracellular Loop. Cunha, E.S., Sfriso, P., Rojas, A.L. et al. Structure (2017) 25:53-65. DOI 10.1016/j.str.2016.11.003 · PubMed
Other PDB entries of the same protein (UniProt P60033 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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