Structure of PDB 7n1r Chain B Binding Site BS01

Receptor Information
>7n1r Chain B (length=606) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGE
RLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKK
TKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVP
AYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVF
DLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKK
TGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLT
RAKFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQ
LVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLT
LGIETVGGVMTKLIPRNTVVPTKKSQIFSVGGTVTIKVYEGERPLTKDNH
LLGTFDLTGIPPAPRGVPQIEVTFEIDVNGILRVTAEDKGTGNKNKITIT
NDQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIG
DKEKLGGKLSSEDKETMEKAVEEKIEWLESHQDADIEDFKAKKKELEEIV
QPIISK
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain7n1r Chain B Residue 703 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB7n1r A novel and unique ATP hydrolysis to AMP by a human Hsp70 Binding immunoglobin protein (BiP).
Resolution2.03 Å
Binding residue
(original residue number in PDB)		G36 T38 G227
Binding residue
(residue number reindexed from 1)		G13 T15 G204
Annotation score1
Enzymatic activity
Enzyme Commision number 3.6.4.10: non-chaperonin molecular chaperone ATPase.
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:7n1r, PDBe:7n1r, PDBj:7n1r
PDBsum7n1r
PubMed34941000
UniProtP11021|BIP_HUMAN Endoplasmic reticulum chaperone BiP (Gene Name=HSPA5)

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