T13G Mutant of the ATPASE fragment of Bovine HSC70. Determined by X-ray diffraction at 1.7 Å resolution. Released 16 Sept 1998.
Explore 2BUP in 3D Show helices and sheets RCSB PDB PDBe
2BUP contains 18 α-helices and 20 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 |
|---|---|---|---|
| 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 | |
| α-helix | 63-65 | 3 | |
| 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 | |
| α-helix | 357-359 | 3 | |
| β-strand | 360 | 1 | 5 |
| α-helix | 368-380 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Heat shock cognate 71 kDa protein | A | protein | 381 | Bos taurus | P19120 (AlphaFold model) |
>2BUP_1 Heat shock cognate 71 kDa protein (chains A) MSKGPAVGIDLGGTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVA MNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVS SMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAA IAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNH FIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRA RFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELN KSINPDEAVAYGAAVQAAILS
| ID | Name | Formula | Copies |
|---|---|---|---|
| PO4 | Phosphate ion | O4 P | 1 |
| MG | Magnesium ion | Mg | 1 |
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 1 |
| ATP | Adenosine-5'-triphosphate | C10 H16 N5 O13 P3 | 1 |
Water and common crystallization additives (K, CL) are not listed.
The hydroxyl of threonine 13 of the bovine 70-kDa heat shock cognate protein is essential for transducing the ATP-induced conformational change. Sousa, M.C., McKay, D.B. Biochemistry (1998) 37:15392-15399. DOI 10.1021/bi981510x · 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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