Structure of PDB 5opx Chain I Binding Site BS02

Receptor Information
>5opx Chain I (length=520) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AAKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITK
DGVSVAREIELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIIT
EGLKAVACGMNPMDLKRGIDKAVTAAVEELKALSVPCSDSKAIAQVGTIS
ANSDETVGKLIAEAMDKVGKEGVITVEDGTGLQDELDVVMQFDRGYLSPY
FINKPETGAVELESPFILLADKKISNIREMLPVLEAVAKAGKPLLIIAED
VEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVISE
EIGMELEKATLEDLGQAKRVVINKDTTTIIDGVGEEAAIQGRVAQIRQQI
EEATSDYDREKLQERVAKLAVAVIKVGAATEVEMKEKKARVEDALHATRA
AVEEGVVAGGGVALIRVASKLADLRGQNEDQNVGIKVALRAMEAPLRQIV
LNCGEEPSVVANTVKGGDGNYGYNAATEEYGNMIDMGILDPTKVTRSALQ
YAASVAGLMITTECMVTDLP
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 chain5opx Chain I Residue 602 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5opx GroEL Ring Separation and Exchange in the Chaperonin Reaction.
Resolution3.64 Å
Binding residue
(original residue number in PDB)		D52 D87 T89 D398
Binding residue
(residue number reindexed from 1)		D51 D86 T88 D393
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) D52 T89 T90 D398
Catalytic site (residue number reindexed from 1) D51 T88 T89 D393
Enzyme Commision number 5.6.1.7: chaperonin ATPase.
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
GO:0140662 ATP-dependent protein folding chaperone
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

View graph for
Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5opx, PDBe:5opx, PDBj:5opx
PDBsum5opx
PubMed29336887
UniProtP0A6F5|CH60_ECOLI Chaperonin GroEL (Gene Name=groEL)

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