5AQR: 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 1.91 Å resolution. Released 5 Oct 2016.

Method: X-ray diffraction
Resolution: 1.91 Å
Organism: HOMO SAPIENS
Chains: 6
Atoms: 12,112
Mol. weight: 170.89 kDa
Ligands: N8Y
Released: 5 Oct 2016

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

Secondary structure: helices and β-sheets

5AQR contains 66 α-helices and 64 β-strands across 6 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, 21 β-strands

Element	Residues	Length	Sheet
β-strand	3	1	1
β-strand	7-11	5	2
β-strand	15-22	8	2
β-strand	25-28	4	2
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	81-87	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	138	1	1
β-strand	141-146	6	2
α-helix	152-164	13
β-strand	168-174	7	2
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

Chains B, D and F: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	153-187	35
α-helix	193-201	9
α-helix	204-221	18
α-helix	231-255	25

Chain C: 18 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	3	1	7
β-strand	7-10	4	8
β-strand	15-16	2	9
β-strand	17-22	6	8
β-strand	25-28	4	8
α-helix	29-30	2
β-strand	38-39	2	9
β-strand	42-44	3	10
β-strand	49-51	3	10
α-helix	53-56	4
β-strand	66-67	2	10
α-helix	70-72	3
α-helix	81-87	7
β-strand	93-97	5	11
β-strand	100-107	8	11
β-strand	110-114	5	11
α-helix	116-135	20
β-strand	138	1	7
β-strand	141-146	6	8
α-helix	152-164	13
β-strand	168-174	7	8
α-helix	175-182	8
α-helix	185-187	3
β-strand	193-201	9	12
β-strand	204-213	10	12
β-strand	216-225	10	12
α-helix	230-249	20
α-helix	257-273	17
β-strand	279-288	10	13
β-strand	291-298	8	13
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	12
α-helix	339-342	4
α-helix	344-353	10
α-helix	357-359	3
β-strand	360	1	12
α-helix	368-379	12

Chain E: 18 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	3	1	14
β-strand	7-11	5	15
β-strand	15-22	8	15
β-strand	25-28	4	15
α-helix	29-30	2
β-strand	38-39	2	15
β-strand	42-44	3	16
β-strand	49-51	3	16
α-helix	53-57	5
β-strand	66-67	2	16
α-helix	70-72	3
α-helix	81-87	7
β-strand	93-97	5	17
β-strand	100-107	8	17
β-strand	110-114	5	17
α-helix	116-135	20
β-strand	138	1	14
β-strand	141-146	6	15
α-helix	152-164	13
β-strand	168-174	7	15
α-helix	175-182	8
α-helix	185-187	3
β-strand	193-201	9	18
β-strand	204-213	10	18
β-strand	216-225	10	18
α-helix	230-249	20
α-helix	257-273	17
β-strand	279-288	10	19
β-strand	291-298	8	19
α-helix	299-305	7
α-helix	307-311	5
α-helix	314-323	10
α-helix	328-330	3
β-strand	333-337	5	18
α-helix	339-342	4
α-helix	344-353	10
α-helix	357-359	3
β-strand	360	1	18
α-helix	368-379	12

Molecules and chains

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

Sequence of entity 1 (A, C, E), FASTA

>5AQR_1 HEAT SHOCK COGNATE 71 KDA PROTEIN (chains A, C, E)
GPLGSMSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAA
KNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFY
PEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINE
PTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDN
RMVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYT
SITRARFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFN
GKELNKSINPDEAVAYGAAVQAAILS

Sequence of entity 2 (B, D, F), FASTA

>5AQR_2 BAG FAMILY MOLECULAR CHAPERONE REGULATOR 1 (chains B, D, F)
GPLGSNSPQEEVELKKLKHLEKSVEKIADQLEELNKELTGIQQGFLPKDLQAEALCKLDR
RVKATIEQFMKILEEIDTLILPENFKDSRLKRKGLVKKVQAFLAECDTVEQNICQETE

Ligands and cofactors

ID	Name	Formula	Copies
N8Y	6-methoxyquinazolin-4-amine	C9 H9 N3 O	3

Water and common crystallization additives (TRS, GOL, DMS, CL) 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
5AQV 1.75 Å, Fragment-based screening of HSP70 sheds light on the functional role of ATP-binding site…
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

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