Structure of PDB 8slf Chain B

Receptor sequence
>8slfB (length=436) Species: 1078020 (Mycolicibacterium thermoresistibile ATCC 19527) [Search protein sequence]
ASIIDTVANLAKRRGFVYQSGEIYGGTRSAWDYGPLGVELKENIKRQWWK
SMVTAREDVVGIDTSIILPREVWVASGHVDVFHDPLVECLNCHRRHRQDH
VVCPDCGTWTEPREFNMMLKTYLGPIESDEGLHYLRPETAQGIFTNFANV
VTTARKKPPFGIAQTGKSFRNEITPGNFIFRTREFEQMEMEFFVEPSTAK
EWHQYWIDTRLQWYVDLGIDRDNLRLYEHPPEKLSHYAERTVDIEYKYGF
AGDPWGELEGIANRTDFDLSTHSKHSGVDLSYYDQATDTRYVPYVIEPAA
GLTRSLMAFLIDAYSEDEAPNAKGGVDKRTVLRFDPRLAPVKVAVLPLSR
HADLSPKARDLAAELRQHWNVEFDDAGAIGRRYRRQDEVGTPYCVTVDFD
SLEDNAVTVRERDSMAQERISIDQVTDYLAVRLKGC
3D structure
PDB8slf Crystal Structure of Glycine tRNA ligase from Mycobacterium thermoresistibile (AMP bound)
ChainB
Resolution2.9 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 AMP B R195 F205 T207 F210 E282 L283 E284 A324 G326 R329 R170 F180 T182 F185 E257 L258 E259 A299 G301 R304
BS02 ZN B C90 C125 C128 C89 C103 C106
BS03 MG B V54 R57 V53 R56
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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Biological Process
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Cellular Component
External links
PDB RCSB:8slf, PDBe:8slf, PDBj:8slf
PDBsum8slf
PubMed
UniProtG7CIG9

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