Cryo-EM structure of URAT1(R477S). Determined by electron microscopy at 3.0 Å resolution. Released 28 Aug 2024.
Explore 8WJG in 3D Show helices and sheets RCSB PDB PDBe
8WJG contains 32 α-helices and 8 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 |
|---|---|---|---|
| α-helix | 3-10 | 8 | |
| α-helix | 15-41 | 27 | |
| β-strand | 47-49 | 3 | 1 |
| α-helix | 52-55 | 4 | |
| α-helix | 57-61 | 5 | |
| α-helix | 69-76 | 8 | |
| β-strand | 79 | 1 | 2 |
| α-helix | 81-83 | 3 | |
| β-strand | 85 | 1 | 2 |
| α-helix | 86 | 1 | |
| β-strand | 90-91 | 2 | 3 |
| α-helix | 96-99 | 4 | |
| α-helix | 110-112 | 3 | |
| β-strand | 113-114 | 2 | 3 |
| β-strand | 120-122 | 3 | 1 |
| β-strand | 129 | 1 | 4 |
| α-helix | 131-135 | 5 | |
| α-helix | 139-141 | 3 | |
| α-helix | 144-170 | 27 | |
| α-helix | 172-191 | 20 | |
| α-helix | 196-224 | 29 | |
| α-helix | 230-254 | 25 | |
| β-strand | 257 | 1 | 4 |
| α-helix | 258-266 | 9 | |
| α-helix | 268-276 | 9 | |
| α-helix | 280-281 | 2 | |
| α-helix | 283-288 | 6 | |
| α-helix | 292-305 | 14 | |
| α-helix | 309-312 | 4 | |
| α-helix | 317-328 | 12 | |
| α-helix | 337-342 | 6 | |
| α-helix | 344-367 | 24 | |
| α-helix | 371-374 | 4 | |
| α-helix | 378-402 | 25 | |
| α-helix | 405-425 | 21 | |
| α-helix | 433-459 | 27 | |
| α-helix | 462-489 | 28 | |
| α-helix | 496-512 | 17 | |
| α-helix | 522-524 | 3 | |
| α-helix | 527-537 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Solute carrier family 22 member 12 | A | protein | 538 | Homo sapiens | Q96S37 (AlphaFold model) |
>8WJG_1 Solute carrier family 22 member 12 (chains A) MAFSELLDLVGGLGRFQVLQTMALMVSIMWLCTQSMLENFSAAVPSHRCWAPLLDNSTAQ ASILGSLSPEALLAISIPPGPNQRPHQCRRFRQPQWQLLDPNATATSWSEADTEPCVDGW VYDRSIFTSTIVAKWNLVCDSHALKPMAQSIYLAGILVGAAACGPASDRFGRRLVLTWSY LQMAVMGTAAAFAPAFPVYCLFRFLLAFAVAGVMMNTGTLLMEWTAARARPLVMTLNSLG FSFGHGLTAAVAYGVRDWTLLQLVVSVPFFLCFLYSWWLAESARWLLTTGRLDWGLQELW RVAAINGKGAVQDTLTPEVLLSAMREELSMGQPPASLGTLLRMPGLRFRTCISTLCWFAF GFTFFGLALDLQALGSNIFLLQMFIGVVDIPAKMGALLLLSHLGRRPTLAASLLLAGLCI LANTLVPHEMGALRSALAVLGLGGVGAAFTCITIYSSELFPTVLRMTAVGLGQMAASGGA ILGPLVRLLGVHGPWLPLLVYGTVPVLSGLAALLLPETQSLPLPDTIQDVQNQAVKKA
Structural basis for the transport and substrate selection of human urate transporter 1. He, J., Liu, G., Kong, F. et al. Cell Rep (2024) 43:114628-114628. DOI 10.1016/j.celrep.2024.114628 · PubMed
Other PDB entries of the same protein (UniProt Q96S37 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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