Structure of PDB 6mrd Chain A

Receptor sequence
>6mrdA (length=528) Species: 9606 (Homo sapiens) [Search protein sequence]
GSAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVT
KDGVTVAKSIDLKDKYKNIGAKLVQDVANNTNEEAGDGTTTATVLARSIA
KEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATI
SANGDKEIGNIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYI
SPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIANAHRKPLVII
AEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAV
FGEEGLTLNLEDVQPHDLGKVGEVIVTKDDAMLLKGKGDKAQIEKRIQEI
IEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDA
LNATRAAVEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKI
PAMTIAKNAGVEGSLIVEKIMQSSSEVGYDAMAGDFVNMVEKGIIDPTKV
VRTALLDAAGVASLLTTAEVVVTEIPKE
3D structure
PDB6mrd Structural basis for active single and double ring complexes in human mitochondrial Hsp60-Hsp10 chaperonin.
ChainA
Resolution3.82 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) D52 T89 T90 D399
Catalytic site (residue number reindexed from 1) D52 T89 T90 D399
Enzyme Commision number 5.6.1.7: chaperonin 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 ADP A G32 P33 D87 G88 T89 T90 G416 D480 I494 D496 G32 P33 D87 G88 T89 T90 G416 D480 I494 D496
Gene Ontology
Molecular Function
GO:0001530 lipopolysaccharide binding
GO:0002039 p53 binding
GO:0003688 DNA replication origin binding
GO:0003697 single-stranded DNA binding
GO:0003723 RNA binding
GO:0003725 double-stranded RNA binding
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0008035 high-density lipoprotein particle binding
GO:0016853 isomerase activity
GO:0016887 ATP hydrolysis activity
GO:0019899 enzyme binding
GO:0031625 ubiquitin protein ligase binding
GO:0034185 apolipoprotein binding
GO:0034186 apolipoprotein A-I binding
GO:0051082 unfolded protein binding
GO:0051087 protein-folding chaperone binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0002755 MyD88-dependent toll-like receptor signaling pathway
GO:0002842 positive regulation of T cell mediated immune response to tumor cell
GO:0006457 protein folding
GO:0006458 'de novo' protein folding
GO:0006919 activation of cysteine-type endopeptidase activity involved in apoptotic process
GO:0006986 response to unfolded protein
GO:0008637 apoptotic mitochondrial changes
GO:0009409 response to cold
GO:0032727 positive regulation of interferon-alpha production
GO:0032729 positive regulation of type II interferon production
GO:0032733 positive regulation of interleukin-10 production
GO:0032735 positive regulation of interleukin-12 production
GO:0032755 positive regulation of interleukin-6 production
GO:0034514 mitochondrial unfolded protein response
GO:0042026 protein refolding
GO:0042100 B cell proliferation
GO:0042110 T cell activation
GO:0042113 B cell activation
GO:0043032 positive regulation of macrophage activation
GO:0043065 positive regulation of apoptotic process
GO:0043066 negative regulation of apoptotic process
GO:0044406 adhesion of symbiont to host
GO:0045041 protein import into mitochondrial intermembrane space
GO:0048291 isotype switching to IgG isotypes
GO:0050821 protein stabilization
GO:0050870 positive regulation of T cell activation
GO:0051131 chaperone-mediated protein complex assembly
GO:0051604 protein maturation
GO:0051702 biological process involved in interaction with symbiont
GO:0098761 cellular response to interleukin-7
Cellular Component
GO:0005615 extracellular space
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005743 mitochondrial inner membrane
GO:0005759 mitochondrial matrix
GO:0005769 early endosome
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0005905 clathrin-coated pit
GO:0009986 cell surface
GO:0016020 membrane
GO:0030135 coated vesicle
GO:0030141 secretory granule
GO:0032991 protein-containing complex
GO:0043231 intracellular membrane-bounded organelle
GO:0046696 lipopolysaccharide receptor complex
GO:0070062 extracellular exosome
GO:0097225 sperm midpiece
GO:0097524 sperm plasma membrane
GO:0140494 migrasome

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6mrd, PDBe:6mrd, PDBj:6mrd
PDBsum6mrd
PubMed32317635
UniProtP10809|CH60_HUMAN 60 kDa heat shock protein, mitochondrial (Gene Name=HSPD1)

[Back to BioLiP]