Structure of PDB 3ldq Chain A

Receptor sequence
>3ldqA (length=377) Species: 9606 (Homo sapiens) [Search protein sequence]
PAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDA
AKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQ
VEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQ
RQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGT
FDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDIS
ENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEE
LNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFF
NGKELNKSINPDEAVAYGAAVQAAILS
3D structure
PDB3ldq Adenosine-Derived Inhibitors of 78 kDa Glucose Regulated Protein (Grp78) ATPase: Insights into Isoform Selectivity.
ChainA
Resolution1.9 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 K71 E175 D199
Catalytic site (residue number reindexed from 1) D6 K67 E171 D195
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 3P1 A G202 E268 K271 R272 S275 G339 R342 G198 E264 K267 R268 S271 G335 R338 MOAD: Kd=2.41uM
PDBbind-CN: -logKd/Ki=5.36,Ki=4.32uM
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0140662 ATP-dependent protein folding chaperone

View graph for
Molecular Function
External links
PDB RCSB:3ldq, PDBe:3ldq, PDBj:3ldq
PDBsum3ldq
PubMed21526763
UniProtP11142|HSP7C_HUMAN Heat shock cognate 71 kDa protein (Gene Name=HSPA8)

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