Structure of PDB 8qxt Chain G Binding Site BS02

Receptor Information
>8qxt Chain G (length=524) Species: 469008 (Escherichia coli BL21(DE3)) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AAKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITK
DGVSVAREIELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIIT
EGLKAVAAGMNPMDLKRGIDKAVTAAVEELKALSVPCSDSKAIAQVGTIS
ANSDETVGKLIAEAMDKVGKEGVITVEDGTGLQDELDVVEGMQFDRGYLS
PYFINKPETGAVELESPFILLADKKISNIREMLPVLEAVAKAGKPLLIIA
EDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVI
SEEIGMELEKATLEDLGQAKRVVINKDTTTIIDGVGEEAAIQGRVAQIRQ
QIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALH
ATRAAVEEGVVAGGGVALIRVASKLADLRGQNEDQNVGIKVALRAMEAPL
RQIVLNCGEEPSVVANTVKGGDGNYGYNAATEEYGNMIDMGILDPTKVTR
SALQYAASVAGLMITTECMVTDLP
Ligand information
Ligand IDBEF
InChIInChI=1S/Be.3FH/h;3*1H/q+2;;;/p-3
InChIKeyOGIAHMCCNXDTIE-UHFFFAOYSA-K
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0[Be-](F)(F)F
ACDLabs 10.04
CACTVS 3.341		F[Be-](F)F
FormulaBe F3
NameBERYLLIUM TRIFLUORIDE ION
ChEMBL
DrugBank
ZINC
PDB chain8qxt Chain G Residue 1602 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB8qxt Visualizing chaperonin function in situ by cryo-electron tomography
Resolution2.9 Å
Binding residue
(original residue number in PDB)		D52 G53 D87 T89 T90
Binding residue
(residue number reindexed from 1)		D51 G52 D86 T88 T89
Annotation score1
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016853 isomerase activity
GO:0016887 ATP hydrolysis activity
GO:0042802 identical protein binding
GO:0051082 unfolded protein binding
Biological Process
GO:0006457 protein folding
GO:0009314 response to radiation
GO:0009408 response to heat
GO:0019068 virion assembly
GO:0042026 protein refolding
GO:0051085 chaperone cofactor-dependent protein refolding
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0016020 membrane
GO:1990220 GroEL-GroES complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8qxt, PDBe:8qxt, PDBj:8qxt
PDBsum8qxt
PubMed39169181
UniProtP0A6F5|CH60_ECOLI Chaperonin GroEL (Gene Name=groEL)

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