Structure of PDB 4gri Chain B

Receptor sequence
>4griB (length=485) Species: 224326 (Borreliella burgdorferi B31) [Search protein sequence]
STRVRYAPSPTGLQHIGGIRTALFNYFFAKSCGGKFLLRIEDTDQSRYSP
EAENDLYSSLKWLGISFDEGPVVGGDYAPYVQSQRSAIYKQYAKYLIESG
HAYYCYCSPERLERIKKIQNINKMPPGYDRHCRNLSNEEVENALIKKIKP
VVRFKIPLEGDTSFDDILLGRITWANKDISPDPVILKSDGLPTYHLANVV
DDYLMKITHVLRAQEWVSSGPLHVLLYKAFKWKPPIYCHLPMVMGNDGQK
LSKRHGSTALRQFIEDGYLPEAIINYVTLLGWSYDDKREFFSKNDLEQFF
SIEKINKSPAIFDYHKLDFFNSYYIREKKDEDLFNLLLPFFQKKGYVSKP
STLEENQKLKLLIPLIKSRIKKLSDALNMTKFFYEDIKSWNLDEFLSRKK
TAKEVCSILELIKPILEGFEKRSSEENDKIFYDFAESNLGEILLPIRIAA
LGSKVSPPLFDSLKLIGKSKVFERIKLAQEFLRIN
3D structure
PDB4gri Ligand co-crystallization of aminoacyl-tRNA synthetases from infectious disease organisms.
ChainB
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S11 K255
Catalytic site (residue number reindexed from 1) S9 K253
Enzyme Commision number 6.1.1.17: glutamate--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 ZN B C107 C109 Y130 C134 C105 C107 Y128 C132
BS02 GLU B R7 A9 S11 E43 Y196 R214 W218 R5 A7 S9 E41 Y194 R212 W216
Gene Ontology
Molecular Function
GO:0000049 tRNA binding
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004818 glutamate-tRNA ligase activity
GO:0005524 ATP binding
GO:0008270 zinc ion binding
Biological Process
GO:0006412 translation
GO:0006424 glutamyl-tRNA aminoacylation
GO:0043039 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:4gri, PDBe:4gri, PDBj:4gri
PDBsum4gri
PubMed28303005
UniProtO51345|SYE_BORBU Glutamate--tRNA ligase (Gene Name=gltX)

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