Structure of PDB 6mn8 Chain A Binding Site BS01
Receptor Information
>6mn8 Chain A (length=399) Species:
6282
(Onchocerca volvulus) [
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AHHHHHHIEISKDENYSEWYVQVITKAEMIEYYDISGCYVLRPWSYAIWE
FIQEWFDEEIKKLGVKNCYFPLFVSQSALEKEFAPEVAWITRAGQSDLAE
AIAIRPTSETVMYPSYAKWVQSHRDLPIKLNQWCNVVRWEFKHPTPFLRT
REFLWQEGHTAFQSKDEAEDEVFKILDLYAQIYIDLLAIPVIKGRKGGDF
TATVEAYVPVNGRGIQGATSHHLGQNFSKMFNISFEDPNGGGKIYAWQNS
WGISTRTIGALVMIHGDNCGLVLPPRVATIQMIIVPVGITKDEQKTALIE
KAKEINNKLMDASIRAELDIRDHISPGWKFNHWELKGVPVRIEIGPKDLA
NNQVTCVIRYSGEKRTIPIDGLASKCKDMLEEIHYSMYNRILEVRESHT
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
6mn8 Chain A Residue 601 [
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Receptor-Ligand Complex Structure
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PDB
6mn8
Crystal Structure of Prolyl-tRNA Synthetase from Onchocerca volvulus with bound Halofuginone and nucleotide
Resolution
2.35 Å
Binding residue
(original residue number in PDB)
V172 S293
Binding residue
(residue number reindexed from 1)
V120 S234
Annotation score
1
Enzymatic activity
Enzyme Commision number
6.1.1.15
: proline--tRNA ligase.
Gene Ontology
Molecular Function
GO:0000166
nucleotide binding
GO:0004812
aminoacyl-tRNA ligase activity
GO:0004827
proline-tRNA ligase activity
GO:0005524
ATP binding
GO:0046872
metal ion binding
Biological Process
GO:0006418
tRNA aminoacylation for protein translation
GO:0006433
prolyl-tRNA aminoacylation
Cellular Component
GO:0005737
cytoplasm
GO:0017101
aminoacyl-tRNA synthetase multienzyme complex
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:6mn8
,
PDBe:6mn8
,
PDBj:6mn8
PDBsum
6mn8
PubMed
UniProt
A0A2K6VKP7
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