Structure of PDB 1kog Chain B Binding Site BS03
Receptor Information
>1kog Chain B (length=401) Species:
562
(Escherichia coli) [
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RDHRKIGKQLDLYHMQEEAPGMVFWHNDGWTIFRELEVFVRSKLKEYQYQ
EVKGPFMMDRVLWEKTGHWDNYKDAMFTTSSENREYCIKPMNCPGHVQIF
NQGLKSYRDLPLRMAEFGSCHRNEPSGSLHGLMRVRGFTQDDAHIFCTEE
QIRDEVNGCIRLVYDMYSTFGFEKIVVKLSTRPEKRIGSDEMWDRAEADL
AVALEENNIPFEYQLGEGAFYGPKIEFTLYDCLDRAWQCGTVQLDFSLPS
RLSASYVGEDNERKVPVMIHRAILGSMERFIGILTEEFAGFFPTWLAPVQ
VVIMNITDSQSEYVNELTQKLSNAGIRVKADLRNEKIGFKIREHTLRRVP
YMLVCGDKEVESGKVAVRTRRGKDLGSMDVNEVIEKLQQEIRSRSLKQLE
E
Ligand information
Ligand ID
ZN
InChI
InChI=1S/Zn/q+2
InChIKey
PTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
Formula
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
1kog Chain B Residue 1 [
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Receptor-Ligand Complex Structure
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PDB
1kog
Structural basis of translational control by Escherichia coli threonyl tRNA synthetase.
Resolution
3.5 Å
Binding residue
(original residue number in PDB)
C334 H385 H511
Binding residue
(residue number reindexed from 1)
C93 H144 H270
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
Q381 D383 K465
Catalytic site (residue number reindexed from 1)
Q140 D142 K224
Enzyme Commision number
6.1.1.3
: threonine--tRNA ligase.
Gene Ontology
Molecular Function
GO:0000166
nucleotide binding
GO:0004812
aminoacyl-tRNA ligase activity
GO:0004829
threonine-tRNA ligase activity
GO:0005524
ATP binding
Biological Process
GO:0006418
tRNA aminoacylation for protein translation
GO:0006435
threonyl-tRNA aminoacylation
Cellular Component
GO:0005737
cytoplasm
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:1kog
,
PDBe:1kog
,
PDBj:1kog
PDBsum
1kog
PubMed
11953757
UniProt
P0A8M3
|SYT_ECOLI Threonine--tRNA ligase (Gene Name=thrS)
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