Structure of PDB 5evz Chain B

Receptor sequence
>5evzB (length=381) Species: 9606 (Homo sapiens) [Search protein sequence]
DVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERL
IGDAAKNQTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKP
YIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYF
NDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLG
GGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGK
DVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLTRAK
FEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVK
EFFNGKEPSRGINPDEAVAYGAAVQAGVLSG
3D structure
PDB5evz Probing the ATP Site of GRP78 with Nucleotide Triphosphate Analogs.
ChainB
Resolution1.85 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 K70 E175 D198
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 PO4 B G36 T37 K96 E201 T229 G11 T12 K70 E175 T203
BS02 ADP B T38 Y39 G226 G227 G255 E293 K296 R297 S300 G363 G364 R367 T13 Y14 G200 G201 G229 E267 K270 R271 S274 G337 G338 R341 MOAD: Kd=0.000000064M
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0140662 ATP-dependent protein folding chaperone

View graph for
Molecular Function
External links
PDB RCSB:5evz, PDBe:5evz, PDBj:5evz
PDBsum5evz
PubMed27144892
UniProtP11021|BIP_HUMAN Endoplasmic reticulum chaperone BiP (Gene Name=HSPA5)

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