Prolactin Receptor (PRLR) Complexed with the Natural Hormone (PRL). Determined by X-ray diffraction at 3.35 Å resolution. Released 6 Oct 2010.
Explore 3NPZ in 3D Show helices and sheets RCSB PDB PDBe
3NPZ contains 17 α-helices and 36 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 |
|---|---|---|---|
| α-helix | 15-44 | 30 | |
| α-helix | 69-72 | 4 | |
| α-helix | 77-103 | 27 | |
| α-helix | 114-136 | 23 | |
| α-helix | 164-189 | 26 | |
| α-helix | 190-194 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-7 | 5 | |
| β-strand | 8-13 | 6 | 1 |
| β-strand | 14 | 1 | 2 |
| β-strand | 20-25 | 6 | 1 |
| β-strand | 35-41 | 7 | 3 |
| β-strand | 48-50 | 3 | 3 |
| β-strand | 61-64 | 4 | 1 |
| β-strand | 74-82 | 9 | 3 |
| β-strand | 87-89 | 3 | 3 |
| α-helix | 90-92 | 3 | |
| β-strand | 93-96 | 4 | 3 |
| α-helix | 97-99 | 3 | |
| β-strand | 101 | 1 | 2 |
| α-helix | 103-106 | 4 | |
| β-strand | 107-115 | 9 | 4 |
| β-strand | 121-128 | 8 | 4 |
| β-strand | 142-150 | 9 | 5 |
| β-strand | 157-162 | 6 | 5 |
| β-strand | 166-169 | 4 | 4 |
| α-helix | 172-173 | 2 | |
| β-strand | 177-186 | 10 | 5 |
| α-helix | 193-195 | 3 | |
| β-strand | 198-201 | 4 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9-13 | 5 | 6 |
| β-strand | 14 | 1 | 7 |
| β-strand | 20-24 | 5 | 6 |
| β-strand | 35-40 | 6 | 8 |
| β-strand | 42 | 1 | 9 |
| β-strand | 49-50 | 2 | 8 |
| β-strand | 61-64 | 4 | 6 |
| β-strand | 75-77 | 3 | 9 |
| β-strand | 78-83 | 6 | 8 |
| β-strand | 86-87 | 2 | 8 |
| α-helix | 90-92 | 3 | |
| β-strand | 93-95 | 3 | 9 |
| α-helix | 97-99 | 3 | |
| β-strand | 101 | 1 | 7 |
| α-helix | 103-106 | 4 | |
| β-strand | 107-114 | 8 | 10 |
| β-strand | 122-128 | 7 | 10 |
| β-strand | 143-149 | 7 | 11 |
| β-strand | 157-161 | 5 | 11 |
| β-strand | 166-169 | 4 | 10 |
| β-strand | 177-185 | 9 | 11 |
| α-helix | 189-196 | 8 | |
| β-strand | 198-201 | 4 | 11 |
| α-helix | 202-203 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Prolactin | A | protein | 199 | Homo sapiens | P01236 (AlphaFold model) |
| Prolactin receptor | B, C | protein | 220 | Rattus norvegicus | P05710 (AlphaFold model) |
>3NPZ_1 Prolactin (chains A) LPICPGGAARCQVTLRDLFDRAVVLSHYIHNLSSEMFSEFDKRYTHGRGFITKAINSCHT SSLATPEDKEQAQQMNQKDFLSLIVSILRSWNEPLYHLVTEVRGMQEAPEAILSKAVEIE EQTKRLLEGMELIVSQVHPETKENEIYPVWSGLPSLQMADEESRLSAYYNLLHCLRRDSH KIDNYLKLLKCRIIHNNNC
>3NPZ_2 Prolactin receptor (chains B, C) QSPPGKPEIHKCRSPDKETFTCWWNPGTDGGLPTNYSLTYSKEGEKTTYECPDYKTSGPN SCFFSKQYTSIWKIYIITVNATNQMGSSSSDPLYVDVTYIVEPEPPRNLTLEVKQLKDKK TYLWVKWSPPTITDVKTGWFTMEYEIRLKPEEAEEWEIHFTGHQTQFKVFDLYPGQKYLV QTRCKPDHGYWSRWSQESSVEMPNDFTLKDRSRSHHHHHH
Structural characterization of the stem-stem dimerization interface between prolactin receptor chains complexed with the natural hormone. van Agthoven, J., Zhang, C., Tallet, E. et al. J Mol Biol (2010) 404:112-126. DOI 10.1016/j.jmb.2010.09.036 · PubMed
Other PDB entries of the same protein (UniProt P01236 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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