Structure of PDB 8qxu Chain K

Receptor sequence

>8qxuK (length=525) Species: 469008 (Escherichia coli BL21(DE3))

AAKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITK
DGVSVAREIELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIIT
EGLKAVAAGMNPMDLKRGIDKAVTAAVEELKALSVPCSDSKAIAQVGTIS
ANSDETVGKLIAEAMDKVGKEGVITVEDGTGLQDELDVVEGMQFDRGYLS
PYFINKPETGAVELESPFILLADKKISNIREMLPVLEAVAKAGKPLLIIA
EDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVI
SEEIGMELEKATLEDLGQAKRVVINKDTTTIIDGVGEEAAIQGRVAQIRQ
QIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALH
ATRAAVEEGVVAGGGVALIRVASKLADLRGQNEDQNVGIKVALRAMEAPL
RQIVLNCGEEPSVVANTVKGGDGNYGYNAATEEYGNMIDMGILDPTKVTR
SALQYAASVAGLMITTECMVTDLPK

3D structure

• PDB: 8qxu Visualizing chaperonin function in situ by cryo-electron tomography
• Chain: K
• Resolution: 12.0 Å

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	K	G32 P33 D87 G88 T89 T90 I150 G415 I454 N479 A480 A481 I493 D495	G31 P32 D86 G87 T88 T89 I149 G414 I453 N478 A479 A480 I492 D494
BS02	MG	K	D87 I150 S151	D86 I149 S150

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

External links

• PDB: RCSB:8qxu, PDBe:8qxu, PDBj:8qxu
• PDBsum: 8qxu
• PubMed: 39169181
• UniProt: P0A6F5|CH60_ECOLI Chaperonin GroEL (Gene Name=groEL)