Structure of human MPC IMS-open. Determined by electron microscopy at 3.31 Å resolution. Released 30 Jul 2025.
Explore 9O9T in 3D Show helices and sheets RCSB PDB PDBe
9O9T contains 40 α-helices and 24 β-strands across 2 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 | 25-44 | 20 | |
| α-helix | 53-72 | 20 | |
| α-helix | 78-93 | 16 | |
| β-strand | 128-132 | 5 | 1 |
| α-helix | 139-152 | 14 | |
| β-strand | 156-160 | 5 | 1 |
| α-helix | 165-173 | 9 | |
| β-strand | 181-185 | 5 | 1 |
| α-helix | 186-188 | 3 | |
| α-helix | 189-194 | 6 | |
| β-strand | 198 | 1 | 2 |
| α-helix | 199-201 | 3 | |
| α-helix | 205-210 | 6 | |
| β-strand | 211 | 1 | 3 |
| α-helix | 213-217 | 5 | |
| β-strand | 220-221 | 2 | 4 |
| β-strand | 224-225 | 2 | 4 |
| β-strand | 228-233 | 6 | 1 |
| β-strand | 236-240 | 5 | 5 |
| β-strand | 250 | 1 | 6 |
| α-helix | 253-262 | 10 | |
| β-strand | 267-269 | 3 | 5 |
| α-helix | 276-286 | 11 | |
| β-strand | 293-294 | 2 | 7 |
| β-strand | 297-298 | 2 | 7 |
| α-helix | 304-306 | 3 | |
| α-helix | 308-322 | 15 | |
| α-helix | 332-340 | 9 | |
| β-strand | 344-349 | 6 | 5 |
| α-helix | 351-353 | 3 | |
| α-helix | 354-359 | 6 | |
| β-strand | 364-367 | 4 | 5 |
| α-helix | 368-370 | 3 | |
| β-strand | 371 | 1 | 6 |
| β-strand | 372 | 1 | 8 |
| β-strand | 375 | 1 | 8 |
| α-helix | 376-377 | 2 | |
| β-strand | 380-381 | 2 | 9 |
| β-strand | 382-388 | 7 | 1 |
| β-strand | 389 | 1 | 2 |
| α-helix | 395-400 | 6 | |
| α-helix | 401-406 | 6 | |
| α-helix | 409-418 | 10 | |
| β-strand | 423-424 | 2 | 1 |
| β-strand | 426 | 1 | 3 |
| α-helix | 427-434 | 8 | |
| α-helix | 437-448 | 12 | |
| β-strand | 450-451 | 2 | 9 |
| α-helix | 452-453 | 2 | |
| α-helix | 458-473 | 16 | |
| α-helix | 479-486 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 44-60 | 17 | |
| α-helix | 64-66 | 3 | |
| α-helix | 69-84 | 16 | |
| α-helix | 94-136 | 43 | |
| α-helix | 139-148 | 10 | |
| α-helix | 162-169 | 8 | |
| α-helix | 172-180 | 9 | |
| α-helix | 195-201 | 7 | |
| α-helix | 205-213 | 9 | |
| α-helix | 228-235 | 8 | |
| α-helix | 238-246 | 9 | |
| α-helix | 261-268 | 8 | |
| α-helix | 271-280 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Mitochondrial pyruvate carrier 2 | B | protein | 281 | Homo sapiens | O95563 (AlphaFold model) |
| Mitochondrial pyruvate carrier 1/MBP chimera protein | A | protein | 487 | Homo sapiens, Escherichia coli K-12 | Q9Y5U8 (AlphaFold model) |
>9O9T_1 Mitochondrial pyruvate carrier 2 (chains B) MSAAGARGLRATYHRLLDKVELMLPEKLRPLYNHPAGPRTVFFWAPIMKWGLVCAGLADM ARPAEKLSTAQSAVLMATGFIFSRYSLVIIPKNWSLFAVNFFVGAAGASQLFRIWRYNQE LKAKDLGRKLLEAARAGQLDEVRILLANGADVNAADNTGTTPLHLAAYSGHLEIVEVLLK HGADVDASDVFGYTPLHLAAYWGHLEIVEVLLKNGADVNAMDSDGMTPLHLAAKWGYLEI VEVLLKHGADVNAQDKFGKTAFDISIDNGNEDLAEILQKLN
>9O9T_2 Mitochondrial pyruvate carrier 1/MBP chimera protein (chains A) MAGALVRKAADYVRSKDFRDYLMSTHFWGPVANWGLPIAAINDMKKSPEIISGRMTFALC CYSLTFMRFAYKVQPRNWLLFACHATNEVAQLIQGGRLIKHEMTKTASAGGGGSGGGGSG GGGSEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPD IIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYN KDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDI KDVGVDNAGAKAGLTFLIDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTS KVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKP LGAVALKSYEEELVKDPRVAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVD AALAAAQ
Structure of human mitochondrial pyruvate carrier MPC1 and MPC2 complex. Sun, Y., Wang, Y., Xing, Z. et al. Nat Commun (2025) 16:6700-6700. DOI 10.1038/s41467-025-61939-z · PubMed
Other PDB entries of the same protein (UniProt O95563 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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