Structure of PDB 1b23 Chain P Binding Site BS01
Receptor Information
>1b23 Chain P (length=405) Species:
271
(Thermus aquaticus) [
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AKGEFIRTKPHVNVGTIGHVDHGKTTLTAALTYVAAAENPNVEVKDYGDI
DKAPEERARGITINTAHVEYETAKRHYSHVDCPGHADYIKNMITGAAQMD
GAILVVSAADGPMPQTREHILLARQVGVPYIVVFMNKVDMVDDPELLDLV
EMEVRDLLNQYEFPGDEVPVIRGSALLALEEMHKNPKTKRGENEWVDKIW
ELLDAIDEYIPTPVRDVDKPFLMPVEDVFTITGRGTVATGRIERGKVKVG
DEVEIVGLAPETRKTVVTGVEMHRKTLQEGIAGDNVGLLLRGVSREEVER
GQVLAKPGSITPHTKFEASVYILKKEEGGRHTGFFTGYRPQFYFRTTDVT
GVVRLPQGVEMVMPGDNVTFTVELIKPVALEEGLRFAIREGGRTVGAGVV
TKILE
Ligand information
>1b23 Chain R (length=74) [
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ggcgcguuaacaaagcgguuauguagcggauugcaaauccgucuaguccg
guucgacuccggaacgcgccucca
<<<<<<<..<<<.........>>>.<<<<<<.....>>>>>>....<<<<
<.......>>>>>>>>>>>>....
Receptor-Ligand Complex Structure
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PDB
1b23
The crystal structure of Cys-tRNACys-EF-Tu-GDPNP reveals general and specific features in the ternary complex and in tRNA.
Resolution
2.6 Å
Binding residue
(original residue number in PDB)
I63 N64 Y88 K90 N91 F229 I231 T232 E271 R274 G287 R300 R330 H331 T332 G337 Y338 R339 Q341 T350 I375 K376 E390 G391
Binding residue
(residue number reindexed from 1)
I63 N64 Y88 K90 N91 F229 I231 T232 E271 R274 G287 R300 R330 H331 T332 G337 Y338 R339 Q341 T350 I375 K376 E390 G391
Enzymatic activity
Catalytic site (original residue number in PDB)
K24 T25 T62 H85
Catalytic site (residue number reindexed from 1)
K24 T25 T62 H85
Enzyme Commision number
?
Gene Ontology
Molecular Function
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:1b23
,
PDBe:1b23
,
PDBj:1b23
PDBsum
1b23
PubMed
10368282
UniProt
Q01698
|EFTU_THEAQ Elongation factor Tu (Gene Name=tuf)
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