Structure of PDB 3ldp Chain A

Receptor sequence
>3ldpA (length=381) Species: 9606 (Homo sapiens) [Search protein sequence]
DVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERL
IGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTK
PYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAY
FNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDL
GGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTG
KDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLTRA
KFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLV
KEFFNGKEPSRGINPDEAVAYGAAVQAGVLS
3D structure
PDB3ldp Adenosine-Derived Inhibitors of 78 kDa Glucose Regulated Protein (Grp78) ATPase: Insights into Isoform Selectivity.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D34 K96 E201 D224
Catalytic site (residue number reindexed from 1) D9 K71 E176 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 3P1 A Y39 G227 G255 E293 K296 R297 S300 G364 R367 D391 Y14 G202 G230 E268 K271 R272 S275 G339 R342 D366 MOAD: Kd=2.41uM
PDBbind-CN: -logKd/Ki=5.62,Kd=2.41uM
BindingDB: koff=0.4s-1,Kd=2.41e+3nM
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0140662 ATP-dependent protein folding chaperone

View graph for
Molecular Function
External links
PDB RCSB:3ldp, PDBe:3ldp, PDBj:3ldp
PDBsum3ldp
PubMed21526763
UniProtP11021|BIP_HUMAN Endoplasmic reticulum chaperone BiP (Gene Name=HSPA5)

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