Structure of PDB 7evv Chain A

Receptor sequence
>7evvA (length=489) Species: 5811 (Toxoplasma gondii) [Search protein sequence]
GAMVTAKKDENFSEWYTQAIVRSEMIEYYDISGCYIMRPWAFHIWEKVQR
FFDDEIKKMGVENSYFPMFVSRHKLEKPEVAWVTHYGDSPLPEKIAIRPT
SETIMYPAYAKWIRSHRDLPLKLNQWCSVVRWEFKQPTPFLRTREFLWQE
GHTAHATEEEAWELVLDILELYRRWYEECLAVPVIKGEKSEGEKFAGGKK
TTTVEAFIPENGRGIQAATSHLLGTNFAKMFEIEFEDEEGHKRLVHQTSW
GCTTRSLGVMIMTHGDDKGLVIPPRVASVQVVIIPILFKDENTGEILGKC
RELKTMLEKADIRVRIDDRSNYTPGWKYNHWEVKGVPLRLELGPKDLAKG
TARVVRRDTGEAYQISWADLAPKLLELMEGIQRSLFEKAKARLHEGIEKI
STFDEVMPALNRKHLVLAPWCEDPESEEQIKKETQKLSEIQAIEAGDQVM
TGAMKTLCIPFDQPPMPEGTKCFYTGKPAKRWTLWGRSY
3D structure
PDB7evv Double drugging of prolyl-tRNA synthetase provides a new paradigm for anti-infective drug development.
ChainA
Resolution1.704 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.1.1.15: proline--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 JE6 A R470 E472 K474 L480 R481 T482 F485 W487 Q555 A557 G590 T592 R594 R131 E133 K135 L141 R142 T143 F146 W148 Q216 A218 G251 T253 R255
BS02 PRO A T439 E441 W487 E489 F534 H560 S588 W589 G590 T100 E102 W148 E150 F195 H221 S249 W250 G251
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004827 proline-tRNA ligase activity
GO:0005524 ATP binding
Biological Process
GO:0006418 tRNA aminoacylation for protein translation
GO:0006433 prolyl-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:7evv, PDBe:7evv, PDBj:7evv
PDBsum7evv
PubMed35333915
UniProtA0A7J6JUK2

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