Structure of PDB 6asy Chain A

Receptor sequence
>6asyA (length=606) Species: 9606 (Homo sapiens) [Search protein sequence]
SEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGE
RLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKK
TKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVP
AYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVF
DLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKK
TGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLT
RAKFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQ
LVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLT
LGIETVGGVMTKLIPRNTVVPTKKSQIFSVGGTVTIKVYEGERPLTKDNH
LLGTFDLTGIPPAPRGVPQIEVTFEIDVNGILRVTAEDKGTGNKNKITIT
NDQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIG
DKEKLGGKLSSEDKETMEKAVEEKIEWLESHQDADIEDFKAKKKELEEIV
QPIISK
3D structure
PDB6asy Conformation transitions of the polypeptide-binding pocket support an active substrate release from Hsp70s.
ChainA
Resolution1.85 Å
3D
structure
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Enzymatic activity
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 A G36 T37 T38 Y39 K96 G226 G227 G228 T229 E293 K296 R297 S300 G363 G364 R367 G13 T14 T15 Y16 K73 G203 G204 G205 T206 E270 K273 R274 S277 G340 G341 R344
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6asy, PDBe:6asy, PDBj:6asy
PDBsum6asy
PubMed29084938
UniProtP11021|BIP_HUMAN Endoplasmic reticulum chaperone BiP (Gene Name=HSPA5)

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