Structure of PDB 4pj1 Chain A
Receptor sequence
>4pj1A (length=526) Species:
9606
(Homo sapiens) [
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GSAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVT
KDGVTVAKSIDLKDKYKNIGAKLVQDVANNTNEEAGDGTTTATVLARSIA
KEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATI
SANGDKEIGNIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYI
SPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIANAHRKPLVII
AEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAV
FGEEGLTLNLEDVQPHDLGKVGKVIVTKDDAMLLKGKGDKAQIEKRIQEI
IEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDA
LNATRAAVEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKI
PAMTIAKNAGVEGSLIVEKIMQSSSEVGYDAMAGDFVNMVEKGIIDPTKV
VRTALLDAAGVASLLTTAEVVVTEIP
3D structure
PDB
4pj1
Crystal structure of the human mitochondrial chaperonin symmetrical football complex.
Chain
A
Resolution
3.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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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
M31 P33 D87 G88 T89 T91 G415 G416 I455 D496
M31 P33 D87 G88 T89 T91 G415 G416 I455 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:4pj1
,
PDBe:4pj1
,
PDBj:4pj1
PDBsum
4pj1
PubMed
25918392
UniProt
P10809
|CH60_HUMAN 60 kDa heat shock protein, mitochondrial (Gene Name=HSPD1)
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