Structure of PDB 5e84 Chain F

Receptor sequence
>5e84F (length=606) Species: 9606 (Homo sapiens) [Search protein sequence]
SEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGE
RLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKK
TKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVP
AYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVF
DLGGGAFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKK
TGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLT
RAKFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQ
LVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLT
LGIETVGGVMTKLIPRNTVVPTKKSQIFSVGGTVTIKVYEGERPLTKDNH
LLGTFDLTGIPPAPRGVPQIEVTFEIDVNGILRVTAEDKGTGNKNKITIT
NDQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIG
DKEKLGGKLSSEDKETMEKAVEEKIEWLESHQDADIEDFKAKKKELEEIV
QPIISK
3D structure
PDB5e84 Close and Allosteric Opening of the Polypeptide-Binding Site in a Human Hsp70 Chaperone BiP.
ChainF
Resolution2.99 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D34 K96 E201 D224
Catalytic site (residue number reindexed from 1) D11 K73 E178 D201
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 ATP F G36 T37 T38 Y39 K96 G226 G227 E293 K296 R297 S300 G363 G364 R367 G13 T14 T15 Y16 K73 G203 G204 E270 K273 R274 S277 G340 G341 R344
BS02 MG F D608 D611 D585 D588
BS03 ZN F E201 D224 D231 E178 D201 D208
Gene Ontology
Molecular Function
GO:0005509 calcium ion binding
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016787 hydrolase activity
GO:0016887 ATP hydrolysis activity
GO:0019899 enzyme binding
GO:0019904 protein domain specific binding
GO:0031072 heat shock protein binding
GO:0031625 ubiquitin protein ligase binding
GO:0043022 ribosome binding
GO:0044183 protein folding chaperone
GO:0045296 cadherin binding
GO:0051082 unfolded protein binding
GO:0051087 protein-folding chaperone binding
GO:0051787 misfolded protein binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006983 ER overload response
GO:0021589 cerebellum structural organization
GO:0021680 cerebellar Purkinje cell layer development
GO:0021762 substantia nigra development
GO:0030335 positive regulation of cell migration
GO:0030512 negative regulation of transforming growth factor beta receptor signaling pathway
GO:0030968 endoplasmic reticulum unfolded protein response
GO:0031204 post-translational protein targeting to membrane, translocation
GO:0031333 negative regulation of protein-containing complex assembly
GO:0031398 positive regulation of protein ubiquitination
GO:0034975 protein folding in endoplasmic reticulum
GO:0034976 response to endoplasmic reticulum stress
GO:0035437 maintenance of protein localization in endoplasmic reticulum
GO:0036503 ERAD pathway
GO:0042026 protein refolding
GO:0042149 cellular response to glucose starvation
GO:0043066 negative regulation of apoptotic process
GO:0045944 positive regulation of transcription by RNA polymerase II
GO:0051085 chaperone cofactor-dependent protein refolding
GO:0051603 proteolysis involved in protein catabolic process
GO:0060904 regulation of protein folding in endoplasmic reticulum
GO:0071353 cellular response to interleukin-4
GO:1903891 regulation of ATF6-mediated unfolded protein response
GO:1903894 regulation of IRE1-mediated unfolded protein response
GO:1903895 negative regulation of IRE1-mediated unfolded protein response
GO:1903897 regulation of PERK-mediated unfolded protein response
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005783 endoplasmic reticulum
GO:0005788 endoplasmic reticulum lumen
GO:0005789 endoplasmic reticulum membrane
GO:0005793 endoplasmic reticulum-Golgi intermediate compartment
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0005925 focal adhesion
GO:0008180 COP9 signalosome
GO:0009986 cell surface
GO:0016020 membrane
GO:0030496 midbody
GO:0032991 protein-containing complex
GO:0034663 endoplasmic reticulum chaperone complex
GO:0042470 melanosome
GO:0043231 intracellular membrane-bounded organelle
GO:0070062 extracellular exosome

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5e84, PDBe:5e84, PDBj:5e84
PDBsum5e84
PubMed26655470
UniProtP11021|BIP_HUMAN Endoplasmic reticulum chaperone BiP (Gene Name=HSPA5)

[Back to BioLiP]