Structure of PDB 4p3y Chain A

Receptor sequence
>4p3yA (length=386) Species: 469008 (Escherichia coli BL21(DE3)) [Search protein sequence]
TKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKA
RGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAA
TDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELL
SQYDFPGDDTPIVRGSALKALEGDAEWEAKILELAGFLDSYIPEPERAID
KPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETQKSTCTG
VEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESE
VYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIK
MVVTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVLG
3D structure
PDB4p3y Structure of the Acinetobacter baumannii Dithiol Oxidase DsbA Bound to Elongation Factor EF-Tu Reveals a Novel Protein Interaction Site.
ChainA
Resolution2.154 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D22 K25 T26 T62 H85
Catalytic site (residue number reindexed from 1) D14 K17 T18 T54 H77
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 GDP A D22 G24 K25 T26 T27 N136 K137 D139 M140 S174 L176 D14 G16 K17 T18 T19 N128 K129 D131 M132 S166 L168
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:4p3y, PDBe:4p3y, PDBj:4p3y
PDBsum4p3y
PubMed24860094
UniProtP0CE47|EFTU1_ECOLI Elongation factor Tu 1 (Gene Name=tufA)

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