Structure of PDB 2hdn Chain J

Receptor sequence
>2hdnJ (length=335) Species: 562 (Escherichia coli) [Search protein sequence]
GITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAAT
DGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLS
QYDFPGDDTPIVRGSALKALEGDAEWEAKILELAGFLDSYIPEPERAIDK
PFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETQKSTCTGV
EMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEV
YILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKM
VVTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVLG
3D structure
PDB2hdn Molecular complementarity between tetracycline and the GTPase active site of elongation factor Tu.
ChainJ
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T61 H84
Catalytic site (residue number reindexed from 1) T3 H26
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 J N135 K136 D138 S173 L175 N77 K78 D80 S115 L117
BS02 TAC J T64 S65 D80 C81 P82 T6 S7 D22 C23 P24
Gene Ontology
Molecular Function
GO:0003746 translation elongation factor activity
GO:0003924 GTPase activity
GO:0005525 GTP binding
Biological Process
GO:0006414 translational elongation

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Molecular Function
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Biological Process
External links
PDB RCSB:2hdn, PDBe:2hdn, PDBj:2hdn
PDBsum2hdn
PubMed17057344
UniProtP0CE47|EFTU1_ECOLI Elongation factor Tu 1 (Gene Name=tufA)

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