Structure of PDB 8wuw Chain J

Receptor sequence
>8wuwJ (length=529) Species: 608538 (Hydrogenobacter thermophilus TK-6) [Search protein sequence]
AAKKVIYGEDARARLKAGVDKLANAVKVTLGPRGREVIIEKKWGTPVVTK
DGVTVAKEIEFKDPYENMGAQLVKEVASKTSDVAGDGTTTATVLAQAIFN
EGLRAIASGANPMDIKRGIDKAVETVVNEIKKLSIPVSGRKEIEQVATIS
ANNDATIGKIIADAMEAVGKDGVITVEESKSAETTLETVQGMQFDRGYLS
PYFVTNPDKMEAVLEDPFILIYEKKISNVKDLLPVLENVVRAGKPLLIIA
EDVEAEALATLVVNHIKGVIRACAVKAPGFGQRRKDYLQDIAILTGGTAI
TEELGIKLESVTLDMLGRADKVIVDKDNTTIVGGKGSKEAIQARIEQIKR
QILETTSDYDREKLQERLAKLSGGVAIIRVGAATEAELKEKKARVEDAVH
ATKAAVEEGIVPGGGVALVRASEALDNLKVDNADQQLGIDIIKKACRTPI
RQIAANSGFEGYVVLEKVLQLGKEKGKNWGFDAGVGDYKDMVEAGIIDPT
KVVRVAIQNAASVAGTMLTAEALVAEIPE
3D structure
PDB8wuw Structural insights into thermophilic chaperonin complexes.
ChainJ
Resolution2.6 Å
3D
structure
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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 ANP J L31 G32 P33 V54 D87 G88 T89 T90 T91 G414 G415 D483 A484 I497 D499 L30 G31 P32 V53 D86 G87 T88 T89 T90 G413 G414 D482 A483 I496 D498
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016853 isomerase activity
GO:0051082 unfolded protein binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding
GO:0009408 response to heat
GO:0042026 protein refolding
GO:0051085 chaperone cofactor-dependent protein refolding
Cellular Component
GO:0005737 cytoplasm
GO:1990220 GroEL-GroES complex

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Cellular Component
External links
PDB RCSB:8wuw, PDBe:8wuw, PDBj:8wuw
PDBsum8wuw
PubMed38492570
UniProtD3DK86

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