Structure of PDB 3ruq Chain B

Receptor sequence
>3ruqB (length=516) Species: 39152 (Methanococcus maripaludis) [Search protein sequence]
QPGVLPENMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLG
DVVVTNDGVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGEL
LRKAEELLDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKI
AMTSITGKGAEKAKEKLAEIIVEAVSAVVDDEGKVDKDLIKIEKKSGASI
DDTELIKGVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETETDAEIRIT
DPAKLMEFIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGI
VAARRVKKSDMEKLAKATGANVITNIKDLSAQDLGDAGLVEERKISGDSM
IFVEECKHPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSG
GGSTEVELSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAI
EILVKVRAAHASNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAA
ESTEMLLRIDDVIAAE
3D structure
PDB3ruq Mechanism of nucleotide sensing in group II chaperonins.
ChainB
Resolution2.798 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 B L39 G40 P41 G92 T94 T95 T159 K161 G403 G404 V488 E490 L36 G37 P38 G89 T91 T92 T156 K158 G400 G401 V485 E487
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3ruq, PDBe:3ruq, PDBj:3ruq
PDBsum3ruq
PubMed22193720
UniProtQ877G8

[Back to BioLiP]