Structure of PDB 1a6e Chain A

Receptor sequence
>1a6eA (length=503) Species: 2303 (Thermoplasma acidophilum) [Search protein sequence]
REQGKNAQRNNIEAAKAIADAVRTTLGPKGMDKMLVDSIGDIIISNDGAT
ILKEMDVEHPTAKMIVEVSKAQDTAVGDGTTTAVVLSGELLKQAETLLDQ
GVHPTVISNGYRLAVNEARKIIDEIAEKSTDDATLRKIALTALSGKNTGL
SNDFLADLVVKAVNAVAEVRDGKTIVDTANIKVDKKNGGSVNDTQFISGI
VIDKEKVHSKMPDVVKNAKIALIDSALEIKKTEIEAKVQISDPSKIQDFL
NQETNTFKQMVEKIKKSGANVVLCQKGIDDVAQHYLAKEGIYAVRRVKKS
DMEKLAKATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCKNP
KAVSILIRGGTDHVVSEVERALNDAIRVVAITKEDGKFLWGGGAVEAELA
MRLAKYANSVGGREQLAIEAFAKALEIIPRTLAENAGIDPINTLIKLKAD
DEKGRISVGVDLDNNGVGDMKAKGVVDPLRVKTHALESAVEVATMILRID
DVI
3D structure
PDB1a6e Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT.
ChainA
Resolution3.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D63 T96 T97 D390
Catalytic site (residue number reindexed from 1) D47 T80 T81 D374
Enzyme Commision number ?
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 A L42 G43 P44 D94 G95 T97 T98 T157 S160 G408 L448 V491 D493 L26 G27 P28 D78 G79 T81 T82 T141 S144 G392 L432 V475 D477
BS02 AF3 A T96 T97 D390 T80 T81 D374
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0051082 unfolded protein binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding

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Molecular Function
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Biological Process
External links
PDB RCSB:1a6e, PDBe:1a6e, PDBj:1a6e
PDBsum1a6e
PubMed9546398
UniProtP48424|THSA_THEAC Thermosome subunit alpha (Gene Name=thsA)

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