Structure of PDB 1ha3 Chain B

Receptor sequence
>1ha3B (length=379) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
GEFIRTKPHVNVGTIGHVDHGKTTLTAALTFVTAAENPNAHVEYETAKRH
YSHVDCPGHADYIKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQV
GVPYIVVFMNKVDMVDDPELLDLVEMEVRDLLNQYEFPGDEVPVIRGSAL
LALEQMHRNPKTRRGENEWVDKIWELLDAIDEYIPTPVRDVDKPFLMPVE
DVFTITGRGTVATGRIERGKVKVGDEVEIVGLAPETRKTVVTGVEMHRKT
LQEGIAGDNVGVLLRGVSREEVERGQVLAKPGSITPHTKFEASVYVLKKE
EGGRHTGFFSGYRPQFYFRTTDVTGVVQLPPGVEMVMPGDNVTFTVELIK
PVALEEGLRFAIREGGRTVGAGVVTKILE
3D structure
PDB1ha3 Conformational Change of Elongation Factor TU Induced by Antibiotic Binding: Crystal Structure of the Complex between EF-TU:Gdp and Aurodox
ChainB
Resolution2.0 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 H85
Catalytic site (residue number reindexed from 1) D19 K22 T23 H59
Enzyme Commision number 3.1.5.1: dGTPase.
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 N136 K137 D139 M140 S174 L176 D19 G21 K22 T23 T24 N110 K111 D113 M114 S148 L150
BS02 MAU B I93 L121 R124 Q125 V126 Y161 E162 E327 R385 F386 A387 T394 A397 I67 L95 R98 Q99 V100 Y135 E136 E301 R359 F360 A361 T368 A371
Gene Ontology
Molecular Function
GO:0003723 RNA binding
GO:0003746 translation elongation factor activity
GO:0003924 GTPase activity
GO:0005525 GTP binding
Biological Process
GO:0006412 translation
GO:0006414 translational elongation
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Cellular Component
External links
PDB RCSB:1ha3, PDBe:1ha3, PDBj:1ha3
PDBsum1ha3
PubMed11278992
UniProtQ5SHN6|EFTU1_THET8 Elongation factor Tu-A (Gene Name=tufA)

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