Structure of PDB 8blf Chain M

Receptor sequence

>8blfM (length=525) Species: 562 (Escherichia coli)

AAKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITK
DGVSVAREIELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIIT
EGLKAVAAGMNPMDLKRGIDKAVTAAVEELKALSVPCSDSKAIAQVGTIS
ANSDETVGKLIAEAMDKVGKEGVITVEDGTGLQDELDVVEGMQFDRGYLS
PYFINKPETGAVELESPFILLADKKISNIREMLPVLEAVAKAGKPLLIIA
EDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVI
SEEIGMELEKATLEDLGQAKRVVINKDTTTIIDGVGEEAAIQGRVAQIRQ
QIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALH
ATRAAVEEGVVAGGGVALIRVASKLADLRGQNEDQNVGIKVALRAMEAPL
RQIVLNCGEEPSVVANTVKGGDGNYGYNAATEEYGNMIDMGILDPTKVTR
SALQYAASVAGLMITTECMVTDLPK

3D structure

• PDB: 8blf Time-resolved cryo-EM using a combination of droplet microfluidics with on-demand jetting.
• Chain: M
• Resolution: 3.9 Å

Enzymatic activity

• 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	ATP	M	G32 P33 G53 D87 G88 T89 T90 T91 G414 G415 A480 A481 I493 D495	G31 P32 G52 D86 G87 T88 T89 T90 G413 G414 A479 A480 I492 D494

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

External links

• PDB: RCSB:8blf, PDBe:8blf, PDBj:8blf
• PDBsum: 8blf
• PubMed: 37592181
• UniProt: P0A6F5|CH60_ECOLI Chaperonin GroEL (Gene Name=groEL)