Interleukin 21 receptor. Determined by X-ray diffraction at 2.75 Å resolution. Released 17 Dec 2014.
Explore 4NZD in 3D Show helices and sheets RCSB PDB PDBe
4NZD contains 22 α-helices and 49 β-strands across 3 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 | 4-8 | 5 | 1 |
| β-strand | 14-18 | 5 | 1 |
| β-strand | 49-53 | 5 | 2 |
| β-strand | 58-61 | 4 | 2 |
| β-strand | 74-80 | 7 | 3 |
| β-strand | 87-94 | 8 | 3 |
| α-helix | 95-97 | 3 | |
| β-strand | 99 | 1 | 4 |
| α-helix | 101-104 | 4 | |
| β-strand | 105-111 | 7 | 5 |
| β-strand | 115-120 | 6 | 5 |
| β-strand | 135-143 | 9 | 6 |
| β-strand | 144 | 1 | 7 |
| β-strand | 146 | 1 | 7 |
| α-helix | 151-152 | 2 | |
| β-strand | 153-157 | 5 | 6 |
| β-strand | 163-166 | 4 | 5 |
| α-helix | 168-170 | 3 | |
| β-strand | 176-185 | 10 | 6 |
| α-helix | 186 | 1 | |
| β-strand | 193 | 1 | 4 |
| α-helix | 195-201 | 7 | |
| β-strand | 202-205 | 4 | 6 |
| α-helix | 206-208 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-8 | 5 | 8 |
| β-strand | 13-18 | 6 | 8 |
| β-strand | 27-33 | 7 | 9 |
| β-strand | 39 | 1 | 9 |
| β-strand | 49-53 | 5 | 8 |
| β-strand | 58-63 | 6 | 8 |
| β-strand | 74-80 | 7 | 9 |
| β-strand | 87-94 | 8 | 9 |
| α-helix | 95-97 | 3 | |
| β-strand | 99 | 1 | 8 |
| α-helix | 101-104 | 4 | |
| β-strand | 105-111 | 7 | 10 |
| β-strand | 115-120 | 6 | 10 |
| β-strand | 135-143 | 9 | 11 |
| α-helix | 151-152 | 2 | |
| β-strand | 153-157 | 5 | 11 |
| β-strand | 163-166 | 4 | 10 |
| α-helix | 168-170 | 3 | |
| β-strand | 176-185 | 10 | 11 |
| α-helix | 186 | 1 | |
| β-strand | 193 | 1 | 8 |
| α-helix | 197-201 | 5 | |
| β-strand | 202-205 | 4 | 11 |
| α-helix | 206-207 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-8 | 5 | 12 |
| β-strand | 14-18 | 5 | 12 |
| β-strand | 49-53 | 5 | 13 |
| β-strand | 58-61 | 4 | 13 |
| β-strand | 74-80 | 7 | 14 |
| β-strand | 87-94 | 8 | 14 |
| α-helix | 95-97 | 3 | |
| β-strand | 99 | 1 | 15 |
| α-helix | 101-104 | 4 | |
| β-strand | 105-111 | 7 | 16 |
| β-strand | 115-120 | 6 | 16 |
| β-strand | 135-143 | 9 | 17 |
| α-helix | 151-152 | 2 | |
| β-strand | 153-157 | 5 | 17 |
| β-strand | 163-166 | 4 | 16 |
| α-helix | 168-170 | 3 | |
| β-strand | 176-185 | 10 | 17 |
| α-helix | 186 | 1 | |
| β-strand | 193 | 1 | 15 |
| α-helix | 195-201 | 7 | |
| β-strand | 202-205 | 4 | 17 |
| α-helix | 206-208 | 3 | |
| α-helix | 212 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Interleukin-21 receptor | A, B, C | protein | 219 | Homo sapiens | Q9HBE5 (AlphaFold model) |
>4NZD_1 Interleukin-21 receptor (chains A, B, C) CPDLVCYTDYLQTVICILEMWNLHPSTLTLTWQDQYEELKDEATSCSLHRSAHNATHATY TCHMDVFHFMADDIFSVQITDQSGQYSQECGSFLLAESIKPAPPFDVTVTFSGQYQISWR SDYEDPAFYMLKGKLQYELQYRNRGDPWAVSPRRKLISVDSRSVSLLPLEFRKDSSYELQ VRAGPMPGSSYQGTWSEWSDPVIFQTQSEELKEHHHHHH
Water and common crystallization additives (NA, CL, EDO) are not listed.
Interleukin 21 receptor structure and function. Hamming, O.T., Kang, L., Siupka, P. et al. To be published.
Other PDB entries of the same protein (UniProt Q9HBE5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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