Crystal structure of Tom71. Determined by X-ray diffraction at 1.98 Å resolution. Released 28 Jul 2009.
Explore 3FP3 in 3D Show helices and sheets RCSB PDB PDBe
3FP3 contains 29 α-helices and 0 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 | 112-116 | 5 | |
| α-helix | 120-136 | 17 | |
| α-helix | 147-156 | 10 | |
| α-helix | 161-174 | 14 | |
| α-helix | 177-190 | 14 | |
| α-helix | 195-208 | 14 | |
| α-helix | 211-222 | 12 | |
| α-helix | 229-253 | 25 | |
| α-helix | 263-265 | 3 | |
| α-helix | 266-273 | 8 | |
| α-helix | 278-282 | 5 | |
| α-helix | 295-306 | 12 | |
| α-helix | 310-331 | 22 | |
| α-helix | 338-357 | 20 | |
| α-helix | 361-374 | 14 | |
| α-helix | 378-388 | 11 | |
| α-helix | 395-407 | 13 | |
| α-helix | 412-424 | 13 | |
| α-helix | 428-441 | 14 | |
| α-helix | 447-458 | 12 | |
| α-helix | 462-475 | 14 | |
| α-helix | 481-493 | 13 | |
| α-helix | 496-512 | 17 | |
| α-helix | 521-533 | 13 | |
| α-helix | 545-559 | 15 | |
| α-helix | 564-576 | 13 | |
| α-helix | 580-593 | 14 | |
| α-helix | 597-617 | 21 | |
| α-helix | 620-626 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| TPR repeat-containing protein YHR117W | A | protein | 537 | Saccharomyces cerevisiae | P38825 (AlphaFold model) |
>3FP3_1 TPR repeat-containing protein YHR117W (chains A) GSHMNGEPDIAQLKGLSPSQRQAYAVQLKNRGNHFFTAKNFNEAIKYYQYAIELDPNEPV FYSNISACYISTGDLEKVIEFTTKALEIKPDHSKALLRRASANESLGNFTDAMFDLSVLS LNGDFDGASIEPMLERNLNKQAMKVLNENLSKDEGRGSQVLPSNTSLASFFGIFDSHLEV SSVNTSSNYDTAYALLSDALQRLYSATDEGYLVANDLLTKSTDMYHSLLSANTVDDPLRE NAALALCYTGIFHFLKNNLLDAQVLLQESINLHPTPNSYIFLALTLADKENSQEFFKFFQ KAVDLNPEYPPTYYHRGQMYFILQDYKNAKEDFQKAQSLNPENVYPYIQLACLLYKQGKF TESEAFFNETKLKFPTLPEVPTFFAEILTDRGDFDTAIKQYDIAKRLEEVQEKIHVGIGP LIGKATILARQSSQDPTQLDEEKFNAAIKLLTKACELDPRSEQAKIGLAQLKLQMEKIDE AIELFEDSAILARTMDEKLQATTFAEAAKIQKRLRADPIISAKMELTLARYRAKGML
Molecular chaperone Hsp70/Hsp90 prepares the mitochondrial outer membrane translocon receptor Tom71 for preprotein loading. Li, J., Qian, X., Hu, J. et al. J Biol Chem (2009) 284:23852-23859. DOI 10.1074/jbc.M109.023986 · PubMed
Other PDB entries of the same protein (UniProt P38825 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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