Crystal structure of the eukaryotic ribosome associated complex (RAC), a unique Hsp70/Hsp40 pair. Determined by X-ray diffraction at 3.2 Å resolution. Released 28 Dec 2016.
Explore 5MB9 in 3D Show helices and sheets RCSB PDB PDBe
5MB9 contains 48 α-helices and 63 β-strands across 4 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 | 15-20 | 6 | 1 |
| β-strand | 24-30 | 7 | 1 |
| β-strand | 35-38 | 4 | 1 |
| α-helix | 39 | 1 | |
| β-strand | 47-48 | 2 | 1 |
| β-strand | 50-54 | 5 | 2 |
| β-strand | 57-60 | 4 | 2 |
| α-helix | 62-66 | 5 | |
| β-strand | 75-77 | 3 | 2 |
| α-helix | 80-82 | 3 | |
| α-helix | 94-96 | 3 | |
| α-helix | 99-100 | 2 | |
| β-strand | 101-104 | 4 | 3 |
| β-strand | 107-112 | 6 | 3 |
| α-helix | 121-122 | 2 | |
| β-strand | 123-126 | 4 | 3 |
| α-helix | 127-146 | 20 | |
| β-strand | 152-157 | 6 | 1 |
| α-helix | 163-175 | 13 | |
| β-strand | 179-185 | 7 | 1 |
| α-helix | 186-195 | 10 | |
| β-strand | 205-212 | 8 | 4 |
| β-strand | 217-225 | 9 | 4 |
| β-strand | 228-237 | 10 | 4 |
| α-helix | 242-260 | 19 | |
| α-helix | 265-266 | 2 | |
| α-helix | 267-269 | 3 | |
| α-helix | 271-290 | 20 | |
| β-strand | 293-302 | 10 | 5 |
| β-strand | 305-312 | 8 | 5 |
| α-helix | 313-319 | 7 | |
| α-helix | 321-337 | 17 | |
| α-helix | 342-344 | 3 | |
| β-strand | 347-351 | 5 | 4 |
| α-helix | 353-356 | 4 | |
| α-helix | 358-367 | 10 | |
| β-strand | 373-375 | 3 | 4 |
| α-helix | 389-401 | 13 | |
| α-helix | 406-419 | 14 | |
| β-strand | 421-423 | 3 | 6 |
| β-strand | 426-429 | 4 | 7 |
| β-strand | 430 | 1 | 8 |
| β-strand | 440 | 1 | 8 |
| β-strand | 444 | 1 | 7 |
| α-helix | 448 | 1 | |
| β-strand | 449 | 1 | 6 |
| β-strand | 453-456 | 4 | 9 |
| β-strand | 467-480 | 14 | 7 |
| β-strand | 523-538 | 16 | 7 |
| β-strand | 549-553 | 5 | 9 |
| β-strand | 558-563 | 6 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 15-20 | 6 | 10 |
| β-strand | 24-31 | 8 | 10 |
| β-strand | 34-38 | 5 | 10 |
| α-helix | 39 | 1 | |
| β-strand | 47-48 | 2 | 10 |
| β-strand | 50-54 | 5 | 11 |
| β-strand | 57-60 | 4 | 11 |
| α-helix | 61-66 | 6 | |
| β-strand | 75-77 | 3 | 11 |
| α-helix | 80-82 | 3 | |
| α-helix | 87-89 | 3 | |
| α-helix | 94-96 | 3 | |
| α-helix | 99-101 | 3 | |
| β-strand | 102-104 | 3 | 12 |
| β-strand | 107-112 | 6 | 12 |
| α-helix | 121-122 | 2 | |
| β-strand | 123-126 | 4 | 12 |
| α-helix | 127-146 | 20 | |
| β-strand | 152-157 | 6 | 10 |
| α-helix | 163-175 | 13 | |
| β-strand | 179-185 | 7 | 10 |
| α-helix | 186-195 | 10 | |
| β-strand | 205-212 | 8 | 13 |
| β-strand | 217-225 | 9 | 13 |
| β-strand | 228-237 | 10 | 13 |
| α-helix | 242-260 | 19 | |
| α-helix | 267-269 | 3 | |
| α-helix | 271-290 | 20 | |
| β-strand | 293-302 | 10 | 14 |
| β-strand | 305-312 | 8 | 14 |
| α-helix | 313-319 | 7 | |
| α-helix | 321-337 | 17 | |
| α-helix | 342-344 | 3 | |
| β-strand | 347-351 | 5 | 13 |
| α-helix | 353-356 | 4 | |
| α-helix | 358-367 | 10 | |
| β-strand | 373-375 | 3 | 13 |
| α-helix | 389-401 | 13 | |
| α-helix | 406-411 | 6 | |
| α-helix | 412-416 | 5 | |
| α-helix | 417-419 | 3 | |
| β-strand | 421-423 | 3 | 15 |
| β-strand | 426-429 | 4 | 16 |
| β-strand | 441-444 | 4 | 16 |
| α-helix | 448 | 1 | |
| β-strand | 449 | 1 | 15 |
| β-strand | 453-456 | 4 | 17 |
| β-strand | 471-478 | 8 | 16 |
| β-strand | 525-532 | 8 | 16 |
| β-strand | 547-553 | 7 | 17 |
| β-strand | 559-565 | 7 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 31-33 | 3 | |
| β-strand | 34-36 | 3 | 15 |
| β-strand | 39-40 | 2 | 13 |
| α-helix | 44-56 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 24-28 | 5 | 9 |
| α-helix | 31-33 | 3 | |
| β-strand | 34-36 | 3 | 6 |
| β-strand | 39 | 1 | 4 |
| α-helix | 44-55 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Putative heat shock protein | A, B | protein | 590 | Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) | G0RZX9 (AlphaFold model) |
| Putative ribosome associated protein | C, D | protein | 45 | Chaetomium thermophilum | G0RYD6 (AlphaFold model) |
>5MB9_1 Putative heat shock protein (chains A, B) SAMGWSHPQFEKMAESASKAAPGERVVIGITFGNSNSSIAHTVDDKAEVIANEDGDRQIP TILSYVDGDEYYGQQAKNFLVRNPKNTVAYFRDILGQDFKSVDPTHNHASAHPQEAGDNV VFTIKDKAEEDAEPSTLTVSEIATRYLRRLVGAASEYLGKKVTSAVITIPTNFTEKQKAA LIAAAAAADLEVLQLISEPAAAVLAYDARPEATISDKIIVVADLGGSRSDVTVLASRSGM YTILATVHDYEYHGIALDKVLIDHFSKEFLKKNPGAKDPRENPRSLAKLRLEAESTKRAL SRSTNASFSVESLIDGLDFASTINRLRYETIARTVFEGFNRLVESAVKKAGLDPLDVDEV IMSGGTSNTPRIAANFRYIFPESTRILAPSTDPSALNPSELQARGAALQASLIQEFETED IEQSTHAAVTTMPHVTNAIGVVSVSESGEEKFVPIIAPETAVPARRTVHLDAPKEGGDVL VKVVEGSTHINVIKPEPKAKEDGETKEKTEDADDDGDFDDDDEEEEEEEEEEEKREKVWK IGSTLAEAAVRGVKKGAKVEVTINVNTDLTVIVTAREVGGKGGVRGTLSA
>5MB9_2 Putative ribosome associated protein (chains C, D) GAMAEKDFKAIGKLTQEGSSMRTLEPVGPHFLAHARRVRHKRTFS
Water and common crystallization additives (GOL) are not listed.
Structural insights into a unique Hsp70-Hsp40 interaction in the eukaryotic ribosome-associated complex. Weyer, F.A., Gumiero, A., Gese, G.V. et al. Nat Struct Mol Biol (2017) 24:144-151. DOI 10.1038/nsmb.3349 · PubMed
Other PDB entries of the same protein (UniProt G0RZX9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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