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BioLiP

Structure of PDB 7rak Chain E

Receptor sequence
>7rakE (length=507) Species: 39152 (Methanococcus maripaludis) [Search protein sequence]
MGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTNDGVTIL
REMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGELLRKAEELLDQNV
HPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITGKGAEK
AKEKLAEIIVEAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELIKGVLVD
KERVSAQMPKKVTDAKIALLNCAIEIKETETDAEIRITDPAKLMEFIEQE
EKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVKKSDME
KLAKATGANVITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECKHPKAV
TMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKL
REYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVRAAHAS
NGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLLRIDDV
IAAEKLR
3D structure
PDB7rak CryoEM reveals the stochastic nature of individual ATP binding events in a group II chaperonin.
ChainE
Resolution3.9 Å
3D
structure
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Enzymatic activity
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 ATP E D85 T87 T88 T153 G398 E484 D76 T78 T79 T144 G389 E475
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
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

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