5AQW: 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 1.53 Å resolution. Released 5 Oct 2016.

Method: X-ray diffraction
Resolution: 1.53 Å
Organism: HOMO SAPIENS
Chains: 1
Atoms: 3,468
Mol. weight: 44.49 kDa
Ligands: MG, DTV, PO4, 5P7
Released: 5 Oct 2016

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

Secondary structure: helices and β-sheets

5AQW contains 20 α-helices and 19 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: 20 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	4-6	3
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	53-57	5
α-helix	59-61	3
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
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
β-strand	360	1	4
α-helix	368-383	16

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

>5AQW_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
DTV	(2S,3S)-1,4-dimercaptobutane-2,3-diol	C4 H10 O2 S2	1
PO4	Phosphate ion	O4 P	1
5P7	(1S,2R,3R,5R)-3-(hydroxymethyl)-5-(quinazolin-4-ylamino)cyclopentane-1,2-diol	C14 H17 N3 O3	1

Water and common crystallization additives (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
3Q49 1.54 Å, Crystal structure of the TPR domain of CHIP complexed with Hsp70-C peptide
5AQY 1.56 Å, Fragment-based screening of HSP70 sheds light on the functional role of ATP-binding site…
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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