Structure of PDB 1b23 Chain P Binding Site BS02
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
Ligand ID
CYS
InChI
InChI=1S/C3H7NO2S/c4-2(1-7)3(5)6/h2,7H,1,4H2,(H,5,6)/t2-/m0/s1
InChIKey
XUJNEKJLAYXESH-REOHCLBHSA-N
SMILES
Software
SMILES
CACTVS 3.341
N[CH](CS)C(O)=O
OpenEye OEToolkits 1.5.0
C([C@@H](C(=O)O)N)S
CACTVS 3.341
N[C@@H](CS)C(O)=O
ACDLabs 10.04
O=C(O)C(N)CS
OpenEye OEToolkits 1.5.0
C(C(C(=O)O)N)S
Formula
C3 H7 N O2 S
Name
CYSTEINE
ChEMBL
CHEMBL863
DrugBank
DB00151
ZINC
ZINC000000895042
PDB chain
1b23 Chain R Residue 976 [
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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)
H67 H273 R274 N285
Binding residue
(residue number reindexed from 1)
H67 H273 R274 N285
Annotation score
1
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
View graph for
Molecular Function
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Biological Process
View graph for
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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