6FHK: Heat shock 70 kDa protein 1A

Structure of a modified protein containing a genetically encoded phosphoserine. Determined by X-ray diffraction at 1.66 Å resolution. Released 24 Oct 2018.

Method
X-ray diffraction
Resolution
1.66 Å
Organism
Homo sapiens
Chains
2
Atoms
6,521
Mol. weight
85.36 kDa
Ligands
ADP, PO4, MG
Released
24 Oct 2018

Explore 6FHK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 18 helices, 20 β-strands

ElementResiduesLengthSheet
β-strand7-1041
β-strand15-1622
β-strand17-2261
β-strand25-2841
α-helix29-302
β-strand38-3922
β-strand41-4443
β-strand49-5133
α-helix53-564
α-helix63-653
β-strand66-6833
α-helix70-723
α-helix81-877
β-strand93-9754
β-strand100-10784
β-strand110-11454
α-helix116-13520
β-strand141-14661
α-helix152-16413
β-strand168-17471
α-helix175-1828
β-strand193-20085
β-strand205-21395
β-strand216-225105
α-helix230-24920
α-helix257-27317
β-strand279-288106
β-strand291-29886
α-helix299-3057
α-helix307-3115
α-helix314-32411
α-helix328-3303
β-strand333-33755
α-helix339-3424
α-helix344-35310
α-helix357-3593
β-strand36015
α-helix368-37912
Chain B: 18 helices, 20 β-strands
ElementResiduesLengthSheet
β-strand7-1047
β-strand15-1628
β-strand17-2267
β-strand25-2847
α-helix29-302
β-strand38-3928
β-strand41-4449
β-strand49-5139
α-helix53-564
α-helix63-653
β-strand66-6839
α-helix70-723
α-helix81-877
β-strand93-97510
β-strand100-107810
β-strand110-114510
α-helix116-13520
β-strand141-14667
α-helix152-16413
β-strand168-17477
α-helix175-1828
β-strand193-200811
β-strand205-213911
β-strand216-2251011
α-helix230-24920
α-helix257-27317
β-strand279-284612
β-strand293-298612
α-helix299-3057
α-helix307-3115
α-helix314-32411
α-helix328-3303
β-strand333-337511
α-helix339-3424
α-helix344-35310
β-strand360111
α-helix365-3673
α-helix368-37912

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Heat shock 70 kDa protein 1AA, Bprotein381Homo sapiensP0DMV8 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>6FHK_1 Heat shock 70 kDa protein 1A (chains A, B)
MAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVA
LNPQNSVFDAKRLIGRKFGDPVVQSDMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEIS
SMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAA
IAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNH
FVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRA
RFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLN
KSINPDEAVAYGAAVQAAILM

Ligands and cofactors

IDNameFormulaCopies
ADPAdenosine-5'-diphosphateC10 H15 N5 O10 P22
PO4Phosphate ionO4 P2
MGMagnesium ionMg2

Water and common crystallization additives (K) are not listed.

Primary citation

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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