Structure of PDB 8wuc Chain F

Receptor sequence
>8wucF (length=528) Species: 297 (Hydrogenophilus thermoluteolus) [Search protein sequence]
AAKEVKFHDSARERLVAGVNLLANAVKTTLGPKGRNVVIERSFGAPIVTK
DGVTVAKEIELKDKFENMGAQMVKEVASKTADVAGDGTTTATVLAQAIVR
EGMKYVAAGMNPMDLKRGIDKAVTAIVEELKAISKPCSTTKEIAQVGTIS
ANADSSIGEIIAQAMDKVGKEGVITVEDGKSLENELEVVEGMQFDRGYLS
PYFINNPDKQVAVLDNPYILLHDKKISNIRDLLPVLEQVAKAGRPLLIIA
EDVEGEALATLVVNNLRGILKTCAVKAPGFGDRRKAMLQDIAILTGGTVI
SEEVGLSLEKATLEDLGQAKRVEVAKEHTTIIDGAGDPAKIQARVKEIRV
QIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALH
ATRAAVEEGIVPGGGVALLRAREAAVAKGLKGDNPDQEAGIKIVLRAVEQ
PLREIVANAGEEPSVIVAKVLEGKGNYGYNAATGEFGDMIEMGVLDPTKV
TRSALQNAASVAGLMLTTECMIAEAPKD
3D structure
PDB8wuc Structural insights into thermophilic chaperonin complexes.
ChainF
Resolution2.5 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 ADP F L31 P33 D87 G88 T89 T90 T91 G414 G415 I456 N481 A482 V495 D497 L30 P32 D86 G87 T88 T89 T90 G413 G414 I455 N480 A481 V494 D496
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:8wuc, PDBe:8wuc, PDBj:8wuc
PDBsum8wuc
PubMed38492570
UniProtA0A2Z6DW38

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