Structure of PDB 4pc3 Chain B

Receptor sequence
>4pc3B (length=372) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
TKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGKARGITINTSHVEYDT
PTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILL
GRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVR
GSALKALEGDAEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSIS
GRGTVVTGRVERGIIKVGEEVEIVGIKETQKSTCTGVEMFRKLLDEGRAG
ENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSKDEGGRHTP
FFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDG
LRFAIREGGRTVGAGVVAKVLG
3D structure
PDB4pc3 Structural outline of the detailed mechanism for elongation factor Ts-mediated guanine nucleotide exchange on elongation factor Tu.
ChainB
Resolution1.8313 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H22 K24 T25 T61 H84
Catalytic site (residue number reindexed from 1) H15 K17 T18 T40 H63
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 B D21 G23 K24 T25 T26 N135 K136 M139 S173 A174 L175 D14 G16 K17 T18 T19 N114 K115 M118 S152 A153 L154
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:4pc3, PDBe:4pc3, PDBj:4pc3
PDBsum4pc3
PubMed26073967
UniProtP0CE47|EFTU1_ECOLI Elongation factor Tu 1 (Gene Name=tufA)

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