Structure of PDB 8slg Chain A Binding Site BS02
Receptor Information
>8slg Chain A (length=429) Species:
1078020
(Mycolicibacterium thermoresistibile ATCC 19527) [
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AHHHHASIIDTVANLAKRRGFVYQSGEIYGGTRSAWDYGPLGVELKENIK
RQWWKSMVTAREDVVGIDTSIILPREVWVASGHVDVFHDPLVECLNCHRR
HRQVCPDCGTWTEPREFNMMLKTYLGPIESDEGLHYLRPETAQGIFTNFA
NVVTTARKKPPFGIAQTGKSFRNEITPGNFIFRTREFEQMEMEFFVEPST
AKEWHQYWIDTRLQWYVDLGIDRDNLRLYEHPPEKLSHYAERTVDIEYKY
GFAGDPWGELEGIANRTDFDLSTHSKHSGVDLSYYDQATDTRYVPYVIEP
AAGLTRSLMAFLIDAYSEDEKRTVLRFDPRLAPVKVAVLPLSRHADLSPK
ARDLAAELRQHWNVEFDDAGAIGRRYRRQDEVGTPYCVTVDFDSLEDNAV
TVRERDSMAQERISIDQVTDYLAVRLKGC
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
8slg Chain A Residue 502 [
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Receptor-Ligand Complex Structure
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PDB
8slg
Crystal Structure of Glycine tRNA ligase from Mycobacterium thermoresistibile (glycyl adenylate bound)
Resolution
1.95 Å
Binding residue
(original residue number in PDB)
C90 C125 C128
Binding residue
(residue number reindexed from 1)
C94 C105 C108
Annotation score
1
Enzymatic activity
Enzyme Commision number
6.1.1.14
: glycine--tRNA ligase.
Gene Ontology
Molecular Function
GO:0000166
nucleotide binding
GO:0004812
aminoacyl-tRNA ligase activity
GO:0004820
glycine-tRNA ligase activity
GO:0005524
ATP binding
GO:0046872
metal ion binding
Biological Process
GO:0006412
translation
GO:0006418
tRNA aminoacylation for protein translation
GO:0006426
glycyl-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:8slg
,
PDBe:8slg
,
PDBj:8slg
PDBsum
8slg
PubMed
UniProt
G7CIG9
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