Structure of PDB 3kfb Chain A Binding Site BS02

Receptor Information

>3kfb Chain A (length=509) Species: 39152 (Methanococcus maripaludis)

NMKRYMGRDAQRMNILAGRIIAETVRSTLGPKGMDKMLVDDLGDVVVTND
GVTILREMSVEHPAAKMLIEVAKTQEKEVGDGTTTAVVVAGELLRKAEEL
LDQNVHPTIVVKGYQAAAQKAQELLKTIACEVGAQDKEILTKIAMTSITG
KGAEKAKEKLAEIIVEAVSAVVDDEGKVDKDLIKIEKKSGASIDDTELIK
GVLVDKERVSAQMPKKVTDAKIALLNCAIEIKETETDAEIRITDPAKLME
FIEQEEKMLKDMVAEIKASGANVLFCQKGIDDLAQHYLAKEGIVAARRVK
KSDMEKLAKATGANVITNIKDLSAQDLGDAGLVEERKISGDSMIFVEECK
HPKAVTMLIRGTTEHVIEEVARAVDDAVGVVGCTIEDGRIVSGGGSTEVE
LSMKLREYAEGISGREQLAVRAFADALEVIPRTLAENAGLDAIEILVKVR
AAHASNGNKCAGLNVFTGAVEDMCENGVVEPLRVKTQAIQSAAESTEMLL
RIDDVIAAE

Ligand information

• Ligand ID: MG
• InChI: InChI=1S/Mg/q+2
• InChIKey: JLVVSXFLKOJNIY-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mg+2]
  CACTVS 3.341: [Mg++]
• Formula: Mg
• Name: MAGNESIUM ION
• DrugBank: DB01378
• PDB chain: 3kfb Chain A Residue 545

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3kfb Crystal structures of a group II chaperonin reveal the open and closed states associated with the protein folding cycle.
• Resolution: 3.2 Å
• Binding residue (original residue number in PDB): D91 S157
• Binding residue (residue number reindexed from 1): D81 S147
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): D60 T93 T94 D386
• Catalytic site (residue number reindexed from 1): D50 T83 T84 D376

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

External links

• PDB: RCSB:3kfb, PDBe:3kfb, PDBj:3kfb
• PDBsum: 3kfb
• PubMed: 20573955
• UniProt: Q877G8