Structure of PDB 5evz Chain A

Receptor sequence
>5evzA (length=382) Species: 9606 (Homo sapiens) [Search protein sequence]
DVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERL
IGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTK
PYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAY
FNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDL
GGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTG
KDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLTRA
KFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLV
KEFFNGKEPSRGINPDEAVAYGAAVQAGVLSG
3D structure
PDB5evz Probing the ATP Site of GRP78 with Nucleotide Triphosphate Analogs.
ChainA
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 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 PO4 A G36 T37 K96 E201 T229 G11 T12 K71 E176 T204
BS02 ADP A T38 Y39 G226 G227 G255 E293 K296 R297 S300 G363 G364 R367 T13 Y14 G201 G202 G230 E268 K271 R272 S275 G338 G339 R342 MOAD: Kd=0.000000064M
PDBbind-CN: -logKd/Ki=6.57,Kd=270nM
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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