Structure of PDB 1qqn Chain A

Receptor sequence
>1qqnA (length=378) Species: 9913 (Bos taurus) [Search protein sequence]
GPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGD
AAKNQVAMNPTNTVFDAKRLIGRAFDDAVVQSDMKHWPFMVVNDAGAPKV
QVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGATVTNAVVTVPAYFNDS
QRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKAVGAERNVLIFDLGGG
TFSVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRAHAKDI
SENKRAVRRLATACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFE
ELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDF
FNGKELNKSINPDEAVAYGAAVQAAILS
3D structure
PDB1qqn Mapping the role of active site residues for transducing an ATP-induced conformational change in the bovine 70-kDa heat shock cognate protein.
ChainA
Resolution1.9 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) D7 K68 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 ADP A G12 T14 Y15 G201 G202 G230 E268 K271 R272 S275 G339 R342 D366 G9 T11 Y12 G198 G199 G227 E265 K268 R269 S272 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:1qqn, PDBe:1qqn, PDBj:1qqn
PDBsum1qqn
PubMed10451379
UniProtP19120|HSP7C_BOVIN Heat shock cognate 71 kDa protein (Gene Name=HSPA8)

[Back to BioLiP]