Structure of PDB 5ey4 Chain B

Receptor sequence
>5ey4B (length=380) Species: 9606 (Homo sapiens) [Search protein sequence]
DVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERL
IGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTK
PYIQVDIGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFN
DAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGG
GTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKD
VRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLTRAKF
EELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKE
FFNGKEPSRGINPDEAVAYGAAVQAGVLSG
3D structure
PDB5ey4 Probing the ATP Site of GRP78 with Nucleotide Triphosphate Analogs.
ChainB
Resolution1.86 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 E174 D197
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 DTP B R297 S300 G364 R367 R270 S273 G337 R340 MOAD: Kd=0.00075M
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0140662 ATP-dependent protein folding chaperone

View graph for
Molecular Function
External links
PDB RCSB:5ey4, PDBe:5ey4, PDBj:5ey4
PDBsum5ey4
PubMed27144892
UniProtP11021|BIP_HUMAN Endoplasmic reticulum chaperone BiP (Gene Name=HSPA5)

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