Structure of PDB 3ruw Chain D

Receptor sequence
>3ruwD (length=516) Species: 39152 (Methanococcus maripaludis) [Search protein sequence]
QPGVLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLG
DVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGEL
LRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKI
AMTSITGKGAEKAKEKLAEIIVEAVSAVVDDEGKVDKDLIKIEKKSGASI
DDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETETDAEIRIT
DPAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGI
VAARRVKKSDMEKLAKATGANVIAAIAALSAQDLGDAGLVEERKISGDSM
IFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSG
GGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAI
EILVKVRAAHASNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAA
ESTEMLLRIDDVIAAE
3D structure
PDB3ruw Mechanism of nucleotide sensing in group II chaperonins.
ChainD
Resolution2.702 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 ADP D L39 G40 P41 G92 T94 T95 G160 G403 G404 V488 E490 L36 G37 P38 G89 T91 T92 G157 G400 G401 V485 E487
BS02 AF3 D D60 D91 T93 D57 D88 T90
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:3ruw, PDBe:3ruw, PDBj:3ruw
PDBsum3ruw
PubMed22193720
UniProtQ877G8

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