Structure of PDB 3ruv Chain C

Receptor sequence
>3ruvC (length=516) Species: 39152 (Methanococcus maripaludis) [Search protein sequence]
QPGVLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLG
DVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGEL
LRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKI
AMTSITGKGAEKAKEKLAEIIVEAVSAVVDDEGKVDKDLIKIEKKSGASI
DDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETETDAEIRIT
DPAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGI
VAARRVKKSDMEKLAKATGANVIAAIAALSAQDLGDAGLVEERKISGDSM
IFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSG
GGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAI
EILVKVRAAHASNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAA
ESTEMLLRIDDVIAAE
3D structure
PDB3ruv Mechanism of nucleotide sensing in group II chaperonins.
ChainC
Resolution2.242 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D60 T93 T94 D386
Catalytic site (residue number reindexed from 1) D57 T90 T91 D383
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 ANP C L39 G40 P41 D60 G61 D91 G92 T93 T94 T95 G160 K161 G403 G404 F476 V488 E490 L36 G37 P38 D57 G58 D88 G89 T90 T91 T92 G157 K158 G400 G401 F473 V485 E487
BS02 MG C D60 D386 D57 D383
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
PDB RCSB:3ruv, PDBe:3ruv, PDBj:3ruv
PDBsum3ruv
PubMed22193720
UniProtQ877G8

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