Structure of PDB 5aqh Chain A

Receptor sequence
>5aqhA (length=381) Species: 9606 (Homo sapiens) [Search protein sequence]
MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERL
IGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGR
PKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYF
NDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDL
GGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHK
KDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRA
RFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLL
QDFFNGKELNKSINPDEAVAYGAAVQAAILS
3D structure
PDB5aqh A fragment-based approach applied to a highly flexible target: Insights and challenges towards the inhibition of HSP70 isoforms.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D10 K71 E175 D199
Catalytic site (residue number reindexed from 1) D10 K71 E175 D199
Enzyme Commision number 3.6.4.10: non-chaperonin molecular chaperone ATPase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 ZVO A R272 S275 G339 R342 R272 S275 G339 R342 PDBbind-CN: -logKd/Ki=2.46,Kd=3.5mM
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0140662 ATP-dependent protein folding chaperone

View graph for
Molecular Function
External links
PDB RCSB:5aqh, PDBe:5aqh, PDBj:5aqh
PDBsum5aqh
PubMed27708405
UniProtP11142|HSP7C_HUMAN Heat shock cognate 71 kDa protein (Gene Name=HSPA8)

[Back to BioLiP]