5AQY: Heat shock 70 kda protein 1A

Fragment-based screening of HSP70 sheds light on the functional role of ATP-binding site residues. Determined by X-ray diffraction at 1.56 Å resolution. Released 5 Oct 2016.

Method: X-ray diffraction
Resolution: 1.56 Å
Organism: HOMO SAPIENS
Chains: 1
Atoms: 3,417
Mol. weight: 44.87 kDa
Ligands: MG, ADN
Released: 5 Oct 2016

Explore 5AQY in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5AQY contains 19 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.

Chain A: 19 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	3-6	4
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
α-helix	185-187	3
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	299-312	14
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	368-380	13
α-helix	384-387	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Heat shock 70 kda protein 1A	A	protein	394	HOMO SAPIENS	P0DMV8 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5AQY_1 HEAT SHOCK 70 KDA PROTEIN 1A (chains A)
GPLGSMAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAA
KNQVALNPQNTVFDAKRLIGRKFGDPVVQSDMKHWPFQVINDGDKPKVQVSYKGETKAFY
PEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINE
PTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDN
RLVNHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYT
SITRARFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFN
GRDLNKSINPDEAVAYGAAVQAAILIKSTRAAAS

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	1
ADN	Adenosine	C10 H13 N5 O4	1

Water and common crystallization additives (DMS, EDO) are not listed.

Primary citation

A fragment-based approach applied to a highly flexible target: Insights and challenges towards the inhibition of HSP70 isoforms. Jones, A.M., Westwood, I.M., Osborne, J.D. et al. Sci Rep (2016) 6:34701-34701. DOI 10.1038/srep34701 · PubMed

Other PDB entries of the same protein (UniProt P0DMV8 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5BN8 1.34 Å, Crystal structure of nucleotide-free human Hsp70 NBD.
6K39 1.4 Å, Structural analysis of AIMP2-DX2 and HSP70 interaction
6G3R 1.4 Å, Structure of tellurium-centred Anderson-Evans polyoxotungstate (TEW) bound to the…
6ZYI 1.52 Å, Crystal structure of HSP70 ATPase domain in complex with ADP and calcium
5AQW 1.53 Å, Fragment-based screening of HSP70 sheds light on the functional role of ATP-binding site…
3Q49 1.54 Å, Crystal structure of the TPR domain of CHIP complexed with Hsp70-C peptide
3ATV 1.58 Å, Crystal structure of human Hsp70 NBD in the ADP-bound and Mg ion-free state
3ATU 1.65 Å, Crystal structure of human Hsp70 NBD in the ADP- and Mg ion-bound state
5AQZ 1.65 Å, HSP72 with adenosine-derived inhibitor
6FHK 1.66 Å, Structure of a modified protein containing a genetically encoded phosphoserine
5BN9 1.69 Å, Crystal structure of ADP bound human Hsp70 NBD mutant R272K.
3AY9 1.75 Å, Crystal structure of human Hsp70 NBD in the ADP-, Mg ion-, and K ion-bound state

Browse structure collections

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