Structure of PDB 7fal Chain B

Receptor sequence
>7falB (length=477) Species: 5811 (Toxoplasma gondii) [Search protein sequence]
GAMVTAKKDENFSEWYTQAIVRSEMIEYYDISGCYIMRPWAFHIWEKVQR
FFDDEIKKMGVENSYFPMFVSRHKLEKEPEVAWVTHYGDSPLPEKIAIRP
TSETIMYPAYAKWIRSHRDLPLKLNQWCSVVRWEFKQPTPFLRTREFLWQ
EGHTAHATEEEAWELVLDILELYRRWYEECLAVPVIKGEKSEGEKFAGGK
KTTTVEAFIPENGRGIQAATSHLLGTNFAKMFEIEFEDEEGHKRLVHQTS
WGCTTRSLGVMIMTHGDDKGLVIPPRVASVQVVIIPILTGEILGKCRELK
TMLEKADIRVRIDDRSNYTPGWKYNHWEVKGVPLRLELGPKDLAKGTARV
VRRDTGEAYQISWADLAPKLLELMEGIQRSLFEKAKARLHEGIEKISTFD
EVMPALNRKHLVLAPWCEDPESEEQIKKETQKLSEIVMTGAMKTLCIPFD
QPPMPEGTKCFYTGKPAKRWTLWGRSY
3D structure
PDB7fal Targeting prolyl-tRNA synthetase via a series of ATP-mimetics to accelerate drug discovery against toxoplasmosis.
ChainB
Resolution3.219 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 1T0 B R470 K474 Q475 P476 L480 R481 T482 F485 Q555 G590 C591 T592 R594 R132 K136 Q137 P138 L142 R143 T144 F147 Q217 G252 C253 T254 R256
BS02 PRO B T439 E441 R470 W487 F534 H560 W589 T101 E103 R132 W149 F196 H222 W251
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:7fal, PDBe:7fal, PDBj:7fal
PDBsum7fal
PubMed36854028
UniProtA0A7J6JUK2

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