Disrupted hydrogen bond network impairs ATPase activity in an Hsc70 cysteine mutant. Determined by X-ray diffraction at 1.9 Å resolution. Released 17 Jan 2018.
Explore 6B1M in 3D Show helices and sheets RCSB PDB PDBe
6B1M contains 39 α-helices and 38 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 | 7-11 | 5 | 6 |
| β-strand | 15-22 | 8 | 6 |
| β-strand | 25-28 | 4 | 6 |
| α-helix | 29-30 | 2 | |
| β-strand | 38-39 | 2 | 6 |
| β-strand | 42-44 | 3 | 7 |
| β-strand | 49-51 | 3 | 7 |
| α-helix | 53-56 | 4 | |
| α-helix | 63-65 | 3 | |
| β-strand | 66-67 | 2 | 7 |
| α-helix | 70-72 | 3 | |
| α-helix | 81-87 | 7 | |
| β-strand | 93-97 | 5 | 8 |
| β-strand | 100-107 | 8 | 8 |
| β-strand | 110-114 | 5 | 8 |
| α-helix | 116-135 | 20 | |
| β-strand | 141-146 | 6 | 6 |
| α-helix | 152-164 | 13 | |
| β-strand | 168-174 | 7 | 6 |
| α-helix | 175-182 | 8 | |
| β-strand | 193-200 | 8 | 9 |
| β-strand | 205-213 | 9 | 9 |
| β-strand | 216-225 | 10 | 9 |
| α-helix | 230-249 | 20 | |
| α-helix | 257-273 | 17 | |
| β-strand | 279-288 | 10 | 10 |
| β-strand | 291-298 | 8 | 10 |
| α-helix | 299-305 | 7 | |
| α-helix | 307-312 | 6 | |
| α-helix | 314-324 | 11 | |
| α-helix | 328-330 | 3 | |
| β-strand | 333-337 | 5 | 9 |
| α-helix | 339-342 | 4 | |
| α-helix | 344-353 | 10 | |
| α-helix | 357-359 | 3 | |
| β-strand | 360 | 1 | 9 |
| α-helix | 365-367 | 3 | |
| α-helix | 368-380 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-11 | 5 | 1 |
| β-strand | 15-22 | 8 | 1 |
| β-strand | 25-28 | 4 | 1 |
| α-helix | 29-30 | 2 | |
| β-strand | 38-39 | 2 | 1 |
| β-strand | 42-44 | 3 | 2 |
| β-strand | 49-51 | 3 | 2 |
| α-helix | 53-56 | 4 | |
| α-helix | 63-65 | 3 | |
| β-strand | 66-67 | 2 | 2 |
| α-helix | 70-72 | 3 | |
| α-helix | 81-86 | 6 | |
| α-helix | 87-89 | 3 | |
| β-strand | 93-97 | 5 | 3 |
| β-strand | 100-107 | 8 | 3 |
| β-strand | 110-114 | 5 | 3 |
| 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 | |
| α-helix | 185-187 | 3 | |
| β-strand | 193-200 | 8 | 4 |
| β-strand | 205-213 | 9 | 4 |
| β-strand | 216-225 | 10 | 4 |
| α-helix | 230-249 | 20 | |
| α-helix | 257-273 | 17 | |
| β-strand | 279-288 | 10 | 5 |
| β-strand | 291-298 | 8 | 5 |
| α-helix | 299-305 | 7 | |
| α-helix | 307-312 | 6 | |
| α-helix | 314-324 | 11 | |
| α-helix | 328-330 | 3 | |
| β-strand | 333-337 | 5 | 4 |
| α-helix | 339-342 | 4 | |
| α-helix | 344-353 | 10 | |
| α-helix | 357-359 | 3 | |
| β-strand | 360 | 1 | 4 |
| α-helix | 368-380 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Heat shock protein family A (Hsp70) member 8 | A, B | protein | 400 | Homo Sapiens | P11142 (AlphaFold model) |
>6B1M_1 Heat shock protein family A (Hsp70) member 8 (chains A, B) MGSSHHHHHHSSGLVPRGSHMASPAVGIDLGTTYSWVGVFQHGKVEIIANDQGNRTTPSY VAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRP KVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDA GTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKS TAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQAS IEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGST RIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILS
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 2 |
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 2 |
Water and common crystallization additives (GOL) are not listed.
Disrupted Hydrogen-Bond Network and Impaired ATPase Activity in an Hsc70 Cysteine Mutant. O'Donnell, J.P., Marsh, H.M., Sondermann, H. et al. Biochemistry (2018) 57:1073-1086. DOI 10.1021/acs.biochem.7b01005 · PubMed
Other PDB entries of the same protein (UniProt P11142 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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