Structure of PDB 8ba9 Chain A

Receptor sequence

>8ba9A (length=524) Species: 83333 (Escherichia coli K-12)

AAKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITK
DGVSVAREIELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIIT
EGLKAVAAGMNPMDLKRGIDKAVTAAVEELKALSVPCSDSKAIAQVGTIS
ANSDETVGKLIAEAMDKVGKEGVITVEDGTGLQDELDVVEGMQFDRGYLS
PYFINKPETGAVELESPFILLADKKISNIREMLPVLEAVAKAGKPLLIIA
EDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVI
SEEIGMELEKATLEDLGQAKRVVINKDTTTIIDGVGEEAAIQGRVAQIRQ
QIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALH
ATRAAVEEGVVAGGGVALIRVASKLADLRGQNEDQNVGIKVALRAMEAPL
RQIVLNCGEEPSVVANTVKGGDGNYGYNAATEEYGNMIDMGILDPTKVTR
SALQYAASVAGLMITTECMVTDLP

3D structure

• PDB: 8ba9 Structural basis of substrate progression through the bacterial chaperonin cycle.
• Chain: A
• Resolution: 3.7 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	AF3	A	D87 T89 T90	D86 T88 T89
BS02	ADP	A	D87 G88 T90 T91 I150 G415 N479 A480 I493 D495	D86 G87 T89 T90 I149 G414 N478 A479 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:8ba9, PDBe:8ba9, PDBj:8ba9
• PDBsum: 8ba9
• PubMed: 38064510
• UniProt: P0A6F5|CH60_ECOLI Chaperonin GroEL (Gene Name=groEL)