Structure of PDB 7vc2 Chain B

Receptor sequence
>7vc2B (length=469) Species: 5811 (Toxoplasma gondii) [Search protein sequence]
MVTAKKDENFSEWYTQAIVRSEMIEYYDISGCYIMRPWAFHIWEKVQRFF
DDEIKKMGVENSYFPMFVSVAWVTHYGDSPLPIAIRPTSETIMYPAYAKW
IRSHRDLPLKLNQWCSVVRWEFKQPTPFLRTREFLWQEGHTAHATEEEAW
ELVLDILELYRRWYEECLAVPVIKGEKSEGEKFAGGKKTTTVEAFIPENG
RGIQAATSHLLGTNFAKMFEIEFEDEEGHKRLVHQTSWGCTTRSLGVMIM
THGDDKGLVIPPRVASVQVVIIPILFKDENTGEILGKCRELKTMLEKADI
RVRIDDRSNYTPGWKYNHWEVKGVPLRLELGPKDLAKGTARVVRRDTGEA
YQISWADLAPKLLELMEGIQRSLFEKAKARLHEGIEKISTFDEVMPALNR
KHLVLAPWCEDPESEEQIKKETQKLSEIQATGAMKTLCIPFDQPPMPEGT
KCFYTGKPAKRWTLWGRSY
3D structure
PDB7vc2 Targeting prolyl-tRNA synthetase via a series of ATP-mimetics to accelerate drug discovery against toxoplasmosis.
ChainB
Resolution2.096 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 1UI B R470 E472 K474 Q475 L480 R481 T482 R483 F485 W487 Q555 A557 T592 R594 R119 E121 K123 Q124 L129 R130 T131 R132 F134 W136 Q204 A206 T241 R243
BS02 PRO B T439 E441 W487 E489 F534 H560 W589 G590 T88 E90 W136 E138 F183 H209 W238 G239
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:7vc2, PDBe:7vc2, PDBj:7vc2
PDBsum7vc2
PubMed36854028
UniProtA0A7J6JUK2

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