Structure of PDB 3kfe Chain E

Receptor sequence
>3kfeE (length=487) Species: 39152 (Methanococcus maripaludis) [Search protein sequence]
NMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTND
GVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGELLRKAEEL
LDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITG
KGAEKAKEKLAEIIVEAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELIK
GVLVDKERVSAQMPKKVTDAKIALLNCAIEETASEMLKDMVAEIKASGAN
VLFCQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDL
SAQDLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVAR
AVDDAVGVVGCTIEDGRIVSGGGSTEVELSMKLREYAEGISGREQLAVRA
FADALEVIPRTLAENAGLDAIEILVKVRAAHASNGNKCAGLNVFTGAVED
MCENGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAAE
3D structure
PDB3kfe Crystal structures of a group II chaperonin reveal the open and closed states associated with the protein folding cycle.
ChainE
Resolution3.5 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) D50 T83 T84 D354
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 E G40 D91 G92 T94 T95 G160 G403 G404 E490 G30 D81 G82 T84 T85 G150 G371 G372 E458
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:3kfe, PDBe:3kfe, PDBj:3kfe
PDBsum3kfe
PubMed20573955
UniProtQ877G8

[Back to BioLiP]