5AQI: 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 1.98 Å resolution. Released 5 Oct 2016.

Method: X-ray diffraction
Resolution: 1.98 Å
Organism: HOMO SAPIENS
Chains: 4
Atoms: 7,875
Mol. weight: 113.35 kDa
Ligands: ADE
Released: 5 Oct 2016

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

Secondary structure: helices and β-sheets

5AQI contains 41 α-helices and 42 β-strands across 4 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	2-3	2	1
β-strand	7-10	4	2
β-strand	15-22	8	2
β-strand	25-28	4	2
α-helix	29-30	2
β-strand	37-39	3	2
β-strand	41-44	4	3
β-strand	49-51	3	3
α-helix	53-58	6
β-strand	66-68	3	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	137-138	2	1
β-strand	141-146	6	2
α-helix	152-164	13
β-strand	168-174	7	2
α-helix	175-182	8
β-strand	192-201	10	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	307-311	5
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	368-380	13

Chain B: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	153-188	36
α-helix	193-201	9
α-helix	204-221	18
α-helix	231-257	27

Chain C: 15 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	3	1	7
β-strand	7-10	4	8
β-strand	15-22	8	8
β-strand	25-28	4	8
α-helix	29-31	3
β-strand	37-39	3	8
β-strand	42-44	3	9
β-strand	49-51	3	9
α-helix	53-57	5
β-strand	66-67	2	9
α-helix	70-72	3
α-helix	81-86	6
β-strand	93-97	5	10
β-strand	100-106	7	10
β-strand	111-114	4	10
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
β-strand	193-201	9	11
β-strand	204-213	10	11
β-strand	216-225	10	11
α-helix	230-249	20
α-helix	257-273	17
β-strand	279-288	10	12
β-strand	291-298	8	12
α-helix	299-312	14
α-helix	314-323	10
α-helix	328-330	3
β-strand	333-337	5	11
α-helix	339-342	4
α-helix	344-353	10
β-strand	360	1	11
α-helix	368-379	12

Chain D: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	153-187	35
α-helix	193-202	10
α-helix	204-221	18
α-helix	231-254	24

Molecules and chains

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

Sequence of entity 1 (A, C), FASTA

>5AQI_1 HEAT SHOCK COGNATE 71 KDA PROTEIN (chains A, C)
GPLGSMSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAA
KNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFY
PEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINE
PTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDN
RMVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYT
SITRARFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFN
GKELNKSINPDEAVAYGAAVQAAILS

Sequence of entity 2 (B, D), FASTA

>5AQI_2 BAG FAMILY MOLECULAR CHAPERONE REGULATOR 1 (chains B, D)
GPLGSNSPQEEVELKKLKHLEKSVEKIADQLEELNKELTGIQQGFLPKDLQAEALCKLDR
RVKATIEQFMKILEEIDTLILPENFKDSRLKRKGLVKKVQAFLAECDTVEQNICQETE

Ligands and cofactors

ID	Name	Formula	Copies
ADE	Adenine	C5 H5 N5	2

Water and common crystallization additives (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
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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