Structure of PDB 3kfb Chain A

Receptor sequence
>3kfbA (length=509) Species: 39152 (Methanococcus maripaludis) [Search protein sequence]
NMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTND
GVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGELLRKAEEL
LDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITG
KGAEKAKEKLAEIIVEAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELIK
GVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETETDAEIRITDPAKLME
FIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVK
KSDMEKLAKATGANVITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECK
HPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVE
LSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVR
AAHASNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLL
RIDDVIAAE
3D structure
PDB3kfb Crystal structures of a group II chaperonin reveal the open and closed states associated with the protein folding cycle.
ChainA
Resolution3.2 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 D376
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 A T38 L39 G40 P41 D60 D91 T93 T94 T95 G160 K161 G403 G404 F476 E490 T28 L29 G30 P31 D50 D81 T83 T84 T85 G150 K151 G393 G394 F466 E480
BS02 MG A D91 S157 D81 S147
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:3kfb, PDBe:3kfb, PDBj:3kfb
PDBsum3kfb
PubMed20573955
UniProtQ877G8

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