Structure of PDB 7qpd Chain C

Receptor sequence
>7qpdC (length=364) Species: 9606 (Homo sapiens) [Search protein sequence]
VYFKEQFLDGWTSRWIESKHKSDFGKFVLSSGKFYGDEEKDKGLQTSQDA
RFYALSASFEPFSNKGQTLVVQFTVKHEQNIDCGGGYVKLFPNSLDQTDM
HGDSEYNIMFGPDICGPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLY
TLIVRPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDASKPEDWDER
AKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYK
GEWKPRQIDNPDYKGTWIHPEIDNPEYSPDPSIYAYDNFGVLGLDLWQVK
SGTIFDNFLITNDEAYAEEFGNETWGVTKAAEKQMKDKQDEEQRLKEEEE
DKKRKEEEEAEDKE
3D structure
PDB7qpd Molecular basis of MHC I quality control in the peptide loading complex.
ChainC
Resolution3.73 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 MAN C G89 D118 G84 D113
BS02 GLC C K94 Y111 K89 Y106
Gene Ontology
Molecular Function
GO:0001849 complement component C1q complex binding
GO:0003677 DNA binding
GO:0003723 RNA binding
GO:0003729 mRNA binding
GO:0005049 nuclear export signal receptor activity
GO:0005178 integrin binding
GO:0005506 iron ion binding
GO:0005509 calcium ion binding
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0030246 carbohydrate binding
GO:0031625 ubiquitin protein ligase binding
GO:0042277 peptide binding
GO:0042562 hormone binding
GO:0044183 protein folding chaperone
GO:0046872 metal ion binding
GO:0050681 nuclear androgen receptor binding
GO:0051082 unfolded protein binding
GO:0051087 protein-folding chaperone binding
GO:0140313 molecular sequestering activity
Biological Process
GO:0000122 negative regulation of transcription by RNA polymerase II
GO:0002502 peptide antigen assembly with MHC class I protein complex
GO:0006355 regulation of DNA-templated transcription
GO:0006457 protein folding
GO:0006611 protein export from nucleus
GO:0006874 intracellular calcium ion homeostasis
GO:0007283 spermatogenesis
GO:0008284 positive regulation of cell population proliferation
GO:0009410 response to xenobiotic stimulus
GO:0010595 positive regulation of endothelial cell migration
GO:0010628 positive regulation of gene expression
GO:0017148 negative regulation of translation
GO:0022417 protein maturation by protein folding
GO:0030866 cortical actin cytoskeleton organization
GO:0032355 response to estradiol
GO:0033144 negative regulation of intracellular steroid hormone receptor signaling pathway
GO:0033574 response to testosterone
GO:0034504 protein localization to nucleus
GO:0034975 protein folding in endoplasmic reticulum
GO:0036503 ERAD pathway
GO:0040020 regulation of meiotic nuclear division
GO:0042921 nuclear receptor-mediated glucocorticoid signaling pathway
GO:0042981 regulation of apoptotic process
GO:0045665 negative regulation of neuron differentiation
GO:0045787 positive regulation of cell cycle
GO:0045892 negative regulation of DNA-templated transcription
GO:0048387 negative regulation of retinoic acid receptor signaling pathway
GO:0050766 positive regulation of phagocytosis
GO:0050821 protein stabilization
GO:0051208 sequestering of calcium ion
GO:0055007 cardiac muscle cell differentiation
GO:0071257 cellular response to electrical stimulus
GO:0071285 cellular response to lithium ion
GO:0090398 cellular senescence
GO:0098586 cellular response to virus
GO:1900026 positive regulation of substrate adhesion-dependent cell spreading
GO:1901164 negative regulation of trophoblast cell migration
GO:1901224 positive regulation of non-canonical NF-kappaB signal transduction
GO:1901652 response to peptide
GO:1903416 response to glycoside
GO:1904614 response to biphenyl
GO:2000510 positive regulation of dendritic cell chemotaxis
Cellular Component
GO:0001669 acrosomal vesicle
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005634 nucleus
GO:0005635 nuclear envelope
GO:0005737 cytoplasm
GO:0005764 lysosome
GO:0005783 endoplasmic reticulum
GO:0005788 endoplasmic reticulum lumen
GO:0005789 endoplasmic reticulum membrane
GO:0005790 smooth endoplasmic reticulum
GO:0005829 cytosol
GO:0005840 ribosome
GO:0005925 focal adhesion
GO:0009897 external side of plasma membrane
GO:0009986 cell surface
GO:0012505 endomembrane system
GO:0016020 membrane
GO:0016529 sarcoplasmic reticulum
GO:0030670 phagocytic vesicle membrane
GO:0031410 cytoplasmic vesicle
GO:0032991 protein-containing complex
GO:0033018 sarcoplasmic reticulum lumen
GO:0033116 endoplasmic reticulum-Golgi intermediate compartment membrane
GO:0042824 MHC class I peptide loading complex
GO:0043231 intracellular membrane-bounded organelle
GO:0044194 cytolytic granule
GO:0044322 endoplasmic reticulum quality control compartment
GO:0048471 perinuclear region of cytoplasm
GO:0060473 cortical granule
GO:0062023 collagen-containing extracellular matrix
GO:0070062 extracellular exosome
GO:0071682 endocytic vesicle lumen
GO:0098553 lumenal side of endoplasmic reticulum membrane
GO:0098794 postsynapse
GO:0098978 glutamatergic synapse

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7qpd, PDBe:7qpd, PDBj:7qpd
PDBsum7qpd
PubMed35948544
UniProtP27797|CALR_HUMAN Calreticulin (Gene Name=CALR)

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