Structure of PDB 1ob5 Chain A Binding Site BS01

Receptor Information
>1ob5 Chain A (length=400) Species: 271 (Thermus aquaticus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
IRTKPHVNVGTIGHVDHGKTTLTAALTYVAAAENPNVEVKDYGDIDKAPE
ERARGITINTAHVEYETAKRHYSHVDCPGHADYIKNMITGAAQMDGAILV
VSAADGPMPQTREHILLARQVGVPYIVVFMNKVDMVDDPELLDLVEMEVR
DLLNQYEFPGDEVPVIRGSALLALEEMHKNPKTKRGENEWVDKIWELLDA
IDEYIPTPVRDVDKPFLMPVEDVFTITGRGTVATGRIERGKVKVGDEVEI
VGLAPETRKTVVTGVEMHRKTLQEGIAGDNVGLLLRGVSREEVERGQVLA
KPGSITPHTKFEASVYILKKEEGGRHTGFFTGYRPQFYFRTTDVTGVVRL
PQGVEMVMPGDNVTFTVELIKPVALEEGLRFAIREGGRTVGAGVVTKILE
Ligand information
>1ob5 Chain B (length=77) [Search RNA sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
gcggauuuagcucaguugggagagcgccagacugaagaucuggagguccu
guguucgauccacagaauucgcacaFc
<<<<<<<..<<<<........>>>>.<<<<<.......>>>>>.....<<
<<<.......>>>>>>>>>>>>.....
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1ob5 Enacyloxin Iia Pinpoints a Binding Pocket of Elongation Factor TU for Development of Novel Antibiotics.
Resolution3.1 Å
Binding residue
(original residue number in PDB)
K52 P54 I63 N64 H67 Y88 K90 N91 F229 T230 I231 R234 V237 T239 G269 E271 M272 H273 R274 N285 V286 G287 L289 R295 R300 R330 H331 T332 G337 Y338 R339 Q341 T350 E390 G391 G392
Binding residue
(residue number reindexed from 1)
K47 P49 I58 N59 H62 Y83 K85 N86 F224 T225 I226 R229 V232 T234 G264 E266 M267 H268 R269 N280 V281 G282 L284 R290 R295 R325 H326 T327 G332 Y333 R334 Q336 T345 E385 G386 G387
Enzymatic activity
Catalytic site (original residue number in PDB) D21 K24 T25 T62 H85
Catalytic site (residue number reindexed from 1) D16 K19 T20 T57 H80
Enzyme Commision number 3.6.1.48: Transferred entry: 3.6.5.3.
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1ob5, PDBe:1ob5, PDBj:1ob5
PDBsum1ob5
PubMed16257965
UniProtQ01698|EFTU_THEAQ Elongation factor Tu (Gene Name=tuf)

[Back to BioLiP]