Structure of PDB 3kfk Chain D

Receptor sequence
>3kfkD (length=484) Species: 39152 (Methanococcus maripaludis) [Search protein sequence]
NMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTND
GVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGELLRKAEEL
LDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITG
KGAEKAKEKLAEIIVEAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELVL
VDKERVSAQMPKKVTDAKIALLNCAIEETASEMLKDMVAEIKASGANVLF
CQKGIDDLAQHYLAKEGIVAARRVKKSDMEKLAKATGANVITNIKDLSAQ
DLGDAGLVEERKISGDSMIFVEECKHPKAVTMLIRGTTEHVIEEVARAVD
DAVGVVGCTIEDGRIVSGGGSTEVELSMKLREYAEGISGREQLAVRAFAD
ALEVIPRTLAENAGLDAIEILVKVRAAHASNGNKCAGLNVFTGAVEDMCE
NGVVEPLRVKTQAIQSAAESTEMLLRIDDVIAAE
3D structure
PDB3kfk Crystal structures of a group II chaperonin reveal the open and closed states associated with the protein folding cycle.
ChainD
Resolution6.003 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) D50 T83 T84 D351
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 AGS D D60 D91 G92 T93 G403 G404 V488 E490 D50 D81 G82 T83 G368 G369 V453 E455
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:3kfk, PDBe:3kfk, PDBj:3kfk
PDBsum3kfk
PubMed20573955
UniProtQ877G8

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