Structure of PDB 1ob2 Chain A

Receptor sequence
>1ob2A (length=393) Species: 511693 (Escherichia coli BL21) [Search protein sequence]
AKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQID
NAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDG
AILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVE
MEVRELLSQYDFPGDDTPIVRGSALKALEGDAEWEAKILELAGFLDSYIP
EPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKET
QKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKP
HTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMV
MPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVLS
3D structure
PDB1ob2 Kirromycin Defines a Specific Domain Arrangement of Elongation Factor EF-TU
ChainA
Resolution3.35 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D21 K24 T25 T61 H84
Catalytic site (residue number reindexed from 1) D21 K24 T25 T61 H84
Enzyme Commision number 3.6.1.48: Transferred entry: 3.6.5.3.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0003723 RNA binding
GO:0003746 translation elongation factor activity
GO:0003924 GTPase activity
GO:0005515 protein binding
GO:0005525 GTP binding
GO:0097216 guanosine tetraphosphate binding
Biological Process
GO:0006412 translation
GO:0006414 translational elongation
GO:0046677 response to antibiotic
Cellular Component
GO:0005737 cytoplasm
GO:0005886 plasma membrane
GO:0032045 guanyl-nucleotide exchange factor complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1ob2, PDBe:1ob2, PDBj:1ob2
PDBsum1ob2
PubMed
UniProtP0CE48|EFTU2_ECOLI Elongation factor Tu 2 (Gene Name=tufB)

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