5AQV: Heat shock cognate 71 kda protein

Fragment-based screening of HSP70 sheds light on the functional role of ATP-binding site residues. Determined by X-ray diffraction at 1.75 Å resolution. Released 5 Oct 2016.

Method: X-ray diffraction
Resolution: 1.75 Å
Organism: HOMO SAPIENS
Chains: 2
Atoms: 4,168
Mol. weight: 57.3 kDa
Ligands: KC7
Released: 5 Oct 2016

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

Secondary structure: helices and β-sheets

5AQV contains 22 α-helices and 20 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: 19 helices, 20 β-strands

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	42-44	3	3
β-strand	49-51	3	3
α-helix	53-56	4
β-strand	66-67	2	3
α-helix	70-72	3
α-helix	81-86	6
α-helix	87-89	3
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	193-201	9	5
β-strand	204-213	10	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	307-312	6
α-helix	314-323	10
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

Chain B: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	153-188	36
α-helix	193-221	29
α-helix	231-256	26

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Heat shock cognate 71 kda protein	A	protein	386	HOMO SAPIENS	P11142 (AlphaFold model)
Bag family molecular chaperone regulator 1	B	protein	118	HOMO SAPIENS	Q99933 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5AQV_1 HEAT SHOCK COGNATE 71 KDA PROTEIN (chains A)
GPLGSMSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAA
KNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFY
PEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINE
PTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDN
RMVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYT
SITRARFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFN
GKELNKSINPDEAVAYGAAVQAAILS

Sequence of entity 2 (B), FASTA

>5AQV_2 BAG FAMILY MOLECULAR CHAPERONE REGULATOR 1 (chains B)
GPLGSNSPQEEVELKKLKHLEKSVEKIADQLEELNKELTGIQQGFLPKDLQAEALCKLDR
RVKATIEQFMKILEEIDTLILPENFKDSRLKRKGLVKKVQAFLAECDTVEQNICQETE

Ligands and cofactors

ID	Name	Formula	Copies
KC7	(1R,2S,3R,5R)-3-((5-(benzyloxy)quinazolin-4-yl)amino)-5-(hydroxymethyl)cyclopen…	C21 H23 N3 O4	1

Water and common crystallization additives (TRS, GOL, DMS) 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 P11142 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5AQM 1.63 Å, Fragment-based screening of HSP70 sheds light on the functional role of ATP-binding site…
4H5R 1.64 Å, HSC70 NBD with Na, Cl and glycerol
5AQL 1.69 Å, Fragment-based screening of HSP70 sheds light on the functional role of ATP-binding site…
4H5V 1.75 Å, HSC70 NBD with Mg
6B1N 1.8 Å, Disrupted hydrogen bond network impairs ATPase activity in an Hsc70 cysteine mutant
3AGY 1.85 Å, Crystal structure of human Hsp40 Hdj1 peptide-binding domain complexed with a C-terminal…
6ZYJ 1.85 Å, Crystal structure of Hsc70 ATPase domain in complex with ADP and calcium
4H5N 1.86 Å, HSC70 NBD with PO4, Na, Cl
5AQF 1.88 Å, Fragment-based screening of HSP70 sheds light on the functional role of ATP-binding site…
3LDQ 1.9 Å, Crystal structure of HSC70/BAG1 in complex with small molecule inhibitor
4H5T 1.9 Å, HSC70 NBD with ADP and Mg
5AQT 1.9 Å, Fragment-based screening of HSP70 sheds light on the functional role of ATP-binding site…

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