6K39: PDB entry 6K39

Structural analysis of AIMP2-DX2 and HSP70 interaction. Determined by X-ray diffraction at 1.4 Å resolution. Released 2 Oct 2019.

Method: X-ray diffraction
Resolution: 1.4 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,776
Mol. weight: 33.48 kDa
Released: 2 Oct 2019

Explore 6K39 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6K39 contains 13 α-helices and 22 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: 6 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	396	1	1
β-strand	401-405	5	2
β-strand	409-414	6	2
β-strand	419	1	1
β-strand	422-428	7	3
β-strand	437-444	8	2
β-strand	449	1	2
α-helix	450-452	3
β-strand	454-462	9	2
α-helix	464-466	3
β-strand	474-480	7	3
β-strand	486-492	7	3
β-strand	498-503	6	3
α-helix	506-508	3
α-helix	512-524	13
α-helix	526-535	10
α-helix	536-538	3

Chain B: 7 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	396	1	4
β-strand	401-405	5	5
β-strand	409-414	6	5
β-strand	419	1	4
β-strand	422-428	7	6
β-strand	437-444	8	5
β-strand	449	1	5
α-helix	450-452	3
β-strand	454-462	9	5
α-helix	464-466	3
β-strand	474-480	7	6
β-strand	486-492	7	6
β-strand	498-503	6	6
α-helix	506-508	3
α-helix	512-524	13
α-helix	526-535	10
α-helix	536-538	3
α-helix	541-543	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Heat shock 70 kDa protein 1A,Aminoacyl tRNA synthase complex-interacting multifunctional protein 2	A, B	protein	152	Homo sapiens	P0DMV8 (AlphaFold model), Q13155 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6K39_1 Heat shock 70 kDa protein 1A,Aminoacyl tRNA synthase complex-interacting multifunctional protein 2 (chains A, B)
SDVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDN
NLLGRFELSGIPPAPRGVPQIEVTFDIDANGILNVTATDKSTGKANKITITNDKGRLSKE
EIERMVQEAEKYKAEDEVQRERVSYRLPNVHG

Primary citation

Targeting the interaction of AIMP2-DX2 with HSP70 suppresses cancer development. Lim, S., Cho, H.Y., Kim, D.G. et al. Nat Chem Biol (2020) 16:31-41. DOI 10.1038/s41589-019-0415-2 · 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.
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
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

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