Structure of PDB 1ha3 Chain A

Receptor sequence

>1ha3A (length=391) Species: 300852 (Thermus thermophilus HB8)

GEFIRTKPHVNVGTIGHVDHGKTTLTAALTFVTAAENPNVEVKDYGDIDK
TAHVEYETAKRHYSHVDCPGHADYIKNMITGAAQMDGAILVVSAADGPMP
QTREHILLARQVGVPYIVVFMNKVDMVDDPELLDLVEMEVRDLLNQYEFP
GDEVPVIRGSALLALEQMHRNPKTRRGENEWVDKIWELLDAIDEYIPTPV
RDVDKPFLMPVEDVFTITGRGTVATGRIERGKVKVGDEVEIVGLAPETRK
TVVTGVEMHRKTLQEGIAGDNVGVLLRGVSREEVERGQVLAKPGSITPHT
KFEASVYVLKKEEGGRHTGFFSGYRPQFYFRTTDVTGVVQLPPGVEMVMP
GDNVTFTVELIKPVALEEGLRFAIREGGRTVGAGVVTKILE

3D structure

• PDB: 1ha3 Conformational Change of Elongation Factor TU Induced by Antibiotic Binding: Crystal Structure of the Complex between EF-TU:Gdp and Aurodox
• Chain: A
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D21 K24 T25 H85
• Catalytic site (residue number reindexed from 1): D19 K22 T23 H71
• 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	A	D21 G23 K24 T25 T26 Y47 N136 K137 D139 M140 S174 L176	D19 G21 K22 T23 T24 Y45 N122 K123 D125 M126 S160 L162
BS02	MAU	A	I93 L121 R124 Q125 V126 Y161 E162 E327 R385 F386 A387 T394 A397	I79 L107 R110 Q111 V112 Y147 E148 E313 R371 F372 A373 T380 A383
BS03	MAU	A	R330 H331	R316 H317

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

External links

• PDB: RCSB:1ha3, PDBe:1ha3, PDBj:1ha3
• PDBsum: 1ha3
• PubMed: 11278992
• UniProt: Q5SHN6|EFTU1_THET8 Elongation factor Tu-A (Gene Name=tufA)