Crystal structure of disulfide-bond-crosslinked complex of bovine hsc70 (1-394aa)R171C and bovine Auxilin (810-910aa)D876C in the AMPPNP hydrolyzed form. Determined by X-ray diffraction at 2.21 Å resolution. Released 18 Dec 2007.
Explore 2QWQ in 3D Show helices and sheets RCSB PDB PDBe
2QWQ contains 23 α-helices and 20 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 |
|---|---|---|---|
| β-strand | 7-10 | 4 | 1 |
| β-strand | 15-16 | 2 | 2 |
| β-strand | 17-22 | 6 | 1 |
| β-strand | 25-28 | 4 | 1 |
| α-helix | 29-30 | 2 | |
| β-strand | 38-39 | 2 | 2 |
| β-strand | 42-44 | 3 | 3 |
| β-strand | 49-51 | 3 | 3 |
| α-helix | 53-56 | 4 | |
| β-strand | 66-67 | 2 | 3 |
| α-helix | 70-72 | 3 | |
| α-helix | 81-87 | 7 | |
| β-strand | 93-97 | 5 | 4 |
| β-strand | 100-107 | 8 | 4 |
| β-strand | 110-114 | 5 | 4 |
| α-helix | 116-135 | 20 | |
| β-strand | 141-146 | 6 | 1 |
| α-helix | 152-164 | 13 | |
| β-strand | 168-174 | 7 | 1 |
| α-helix | 175-182 | 8 | |
| β-strand | 193-200 | 8 | 5 |
| β-strand | 205-213 | 9 | 5 |
| β-strand | 216-225 | 10 | 5 |
| α-helix | 230-249 | 20 | |
| α-helix | 257-273 | 17 | |
| β-strand | 279-288 | 10 | 6 |
| β-strand | 291-298 | 8 | 6 |
| α-helix | 299-305 | 7 | |
| α-helix | 307-311 | 5 | |
| α-helix | 314-324 | 11 | |
| α-helix | 328-330 | 3 | |
| β-strand | 333-337 | 5 | 5 |
| α-helix | 339-342 | 4 | |
| α-helix | 344-353 | 10 | |
| β-strand | 360 | 1 | 5 |
| α-helix | 368-379 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 814-826 | 13 | |
| α-helix | 830-834 | 5 | |
| α-helix | 837-839 | 3 | |
| α-helix | 842 | 1 | |
| α-helix | 853-855 | 3 | |
| α-helix | 859-873 | 15 | |
| α-helix | 884-903 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Heat shock cognate 71 kDa protein | A | protein | 394 | Bos taurus | P19120 (AlphaFold model) |
| Putative tyrosine-protein phosphatase auxilin | B | protein | 92 | Bos taurus | Q27974 (AlphaFold model) |
>2QWQ_1 Heat shock cognate 71 kDa protein (chains A) MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVA MNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVS SMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLCIINEPTAAA IAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNH FIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRA RFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELN KSINPDEAVAYGAAVQAAILSGDKSENVQDLLLL
>2QWQ_2 Putative tyrosine-protein phosphatase auxilin (chains B) DPEKLKILEWIEGKERNIRALLSTMHTVLWAGETKWKPVGMADLVTPEQVKKVYRKAVLV VHPCKATGQPYEQYAKMIFMELNDAWSEFENQ
Water and common crystallization additives (ACY, GOL) are not listed.
Structural basis of J cochaperone binding and regulation of Hsp70. Jiang, J., Maes, E.G., Taylor, A.B. et al. Mol Cell (2007) 28:422-433. DOI 10.1016/j.molcel.2007.08.022 · PubMed
Other PDB entries of the same protein (UniProt P19120 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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