Structure of a modified protein containing a genetically encoded phosphoserine. Determined by X-ray diffraction at 1.66 Å resolution. Released 24 Oct 2018.
Explore 6FHK in 3D Show helices and sheets RCSB PDB PDBe
6FHK contains 36 α-helices and 40 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 | 41-44 | 4 | 3 |
| β-strand | 49-51 | 3 | 3 |
| α-helix | 53-56 | 4 | |
| α-helix | 63-65 | 3 | |
| β-strand | 66-68 | 3 | 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 | 368-379 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-10 | 4 | 7 |
| β-strand | 15-16 | 2 | 8 |
| β-strand | 17-22 | 6 | 7 |
| β-strand | 25-28 | 4 | 7 |
| α-helix | 29-30 | 2 | |
| β-strand | 38-39 | 2 | 8 |
| β-strand | 41-44 | 4 | 9 |
| β-strand | 49-51 | 3 | 9 |
| α-helix | 53-56 | 4 | |
| α-helix | 63-65 | 3 | |
| β-strand | 66-68 | 3 | 9 |
| α-helix | 70-72 | 3 | |
| α-helix | 81-87 | 7 | |
| β-strand | 93-97 | 5 | 10 |
| β-strand | 100-107 | 8 | 10 |
| β-strand | 110-114 | 5 | 10 |
| α-helix | 116-135 | 20 | |
| β-strand | 141-146 | 6 | 7 |
| α-helix | 152-164 | 13 | |
| β-strand | 168-174 | 7 | 7 |
| α-helix | 175-182 | 8 | |
| β-strand | 193-200 | 8 | 11 |
| β-strand | 205-213 | 9 | 11 |
| β-strand | 216-225 | 10 | 11 |
| α-helix | 230-249 | 20 | |
| α-helix | 257-273 | 17 | |
| β-strand | 279-284 | 6 | 12 |
| β-strand | 293-298 | 6 | 12 |
| 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 | 11 |
| α-helix | 339-342 | 4 | |
| α-helix | 344-353 | 10 | |
| β-strand | 360 | 1 | 11 |
| α-helix | 365-367 | 3 | |
| α-helix | 368-379 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Heat shock 70 kDa protein 1A | A, B | protein | 381 | Homo sapiens | P0DMV8 (AlphaFold model) |
>6FHK_1 Heat shock 70 kDa protein 1A (chains A, B) MAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVA LNPQNSVFDAKRLIGRKFGDPVVQSDMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEIS SMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAA IAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNH FVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRA RFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLN KSINPDEAVAYGAAVQAAILM
| ID | Name | Formula | Copies |
|---|---|---|---|
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 2 |
| PO4 | Phosphate ion | O4 P | 2 |
| MG | Magnesium ion | Mg | 2 |
Water and common crystallization additives (K) are not listed.
Mitotic phosphorylation regulates Hsp72 spindle localization by uncoupling ATP binding from substrate release. Mukherjee, M., Sabir, S., O'Regan, L. et al. Sci Signal (2018) 11. DOI 10.1126/scisignal.aao2464 · PubMed
Other PDB entries of the same protein (UniProt P0DMV8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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