Structure of PDB 1kax Chain A

Receptor sequence
>1kaxA (length=378) Species: 9913 (Bos taurus) [Search protein sequence]
GPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGD
AAKNQVAMNPTNTVFDAMRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKV
QVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDS
QRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGG
TFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDI
SENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFE
ELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDF
FNGKELNKSINPDEAVAYGAAVQAAILS
3D structure
PDB1kax Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis.
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D10 M71 E175 D199
Catalytic site (residue number reindexed from 1) D7 M68 E172 D196
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 ATP A G12 T13 T14 Y15 G201 G202 T204 E268 K271 R272 S275 G338 G339 R342 D366 G9 T10 T11 Y12 G198 G199 T201 E265 K268 R269 S272 G335 G336 R339 D363
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0140662 ATP-dependent protein folding chaperone

View graph for
Molecular Function
External links
PDB RCSB:1kax, PDBe:1kax, PDBj:1kax
PDBsum1kax
PubMed8663302
UniProtP19120|HSP7C_BOVIN Heat shock cognate 71 kDa protein (Gene Name=HSPA8)

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