Structure of PDB 8slg Chain A

Receptor sequence
>8slgA (length=429) Species: 1078020 (Mycolicibacterium thermoresistibile ATCC 19527) [Search protein sequence]
AHHHHASIIDTVANLAKRRGFVYQSGEIYGGTRSAWDYGPLGVELKENIK
RQWWKSMVTAREDVVGIDTSIILPREVWVASGHVDVFHDPLVECLNCHRR
HRQVCPDCGTWTEPREFNMMLKTYLGPIESDEGLHYLRPETAQGIFTNFA
NVVTTARKKPPFGIAQTGKSFRNEITPGNFIFRTREFEQMEMEFFVEPST
AKEWHQYWIDTRLQWYVDLGIDRDNLRLYEHPPEKLSHYAERTVDIEYKY
GFAGDPWGELEGIANRTDFDLSTHSKHSGVDLSYYDQATDTRYVPYVIEP
AAGLTRSLMAFLIDAYSEDEKRTVLRFDPRLAPVKVAVLPLSRHADLSPK
ARDLAAELRQHWNVEFDDAGAIGRRYRRQDEVGTPYCVTVDFDSLEDNAV
TVRERDSMAQERISIDQVTDYLAVRLKGC
3D structure
PDB8slg Crystal Structure of Glycine tRNA ligase from Mycobacterium thermoresistibile (glycyl adenylate bound)
ChainA
Resolution1.95 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.1.1.14: glycine--tRNA ligase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 G5A A E163 R195 E197 R206 T207 F210 Q212 E214 Y262 E282 L283 E322 A324 G326 R329 E140 R172 E174 R183 T184 F187 Q189 E191 Y239 E259 L260 E299 A301 G303 R306
BS02 ZN A C90 C125 C128 C94 C105 C108
BS03 MG A V54 R57 V60 V58 R61 V64
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
PDBsum8slg
PubMed
UniProtG7CIG9

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