Structure of PDB 8wux Chain D

Receptor sequence
>8wuxD (length=527) Species: 608538 (Hydrogenobacter thermophilus TK-6) [Search protein sequence]
AKKVIYGEDARARLKAGVDKLANAVKVTLGPRGREVIIEKKWGTPVVTKD
GVTVAKEIEFKDPYENMGAQLVKEVASKTSDVAGDGTTTATVLAQAIFNE
GLRAIASGANPMDIKRGIDKAVETVVNEIKKLSIPVSGRKEIEQVATISA
NNDATIGKIIADAMEAVGKDGVITVEESKSAETTLETVQGMQFDRGYLSP
YFVTNPDKMEAVLEDPFILIYEKKISNVKDLLPVLENVVRAGKPLLIIAE
DVEAEALATLVVNHIKGVIRACAVKAPGFGQRRKDYLQDIAILTGGTAIT
EELGIKLESVTLDMLGRADKVIVDKDNTTIVGGKGSKEAIQARIEQIKRQ
ILETTSDYDREKLQERLAKLSGGVAIIRVGAATEAELKEKKARVEDAVHA
TKAAVEEGIVPGGGVALVRASEALDNLKVDNADQQLGIDIIKKACRTPIR
QIAANSGFEGYVVLEKVLQLGKEKGKNWGFDAGVGDYKDMVEAGIIDPTK
VVRVAIQNAASVAGTMLTAEALVAEIP
3D structure
PDB8wux Structural insights into thermophilic chaperonin complexes.
ChainD
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 D P33 K51 D87 G88 T89 T90 T91 G414 G415 D483 A484 I497 D499 P31 K49 D85 G86 T87 T88 T89 G412 G413 D481 A482 I495 D497
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:8wux, PDBe:8wux, PDBj:8wux
PDBsum8wux
PubMed38492570
UniProtD3DK86

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