Structure of PDB 5xiq Chain B

Receptor sequence
>5xiqB (length=480) Species: 508771 (Toxoplasma gondii ME49) [Search protein sequence]
MVTAKKDENFSEWYTQAIVRSEMIEYYDISGCYIMRPWAFHIWEKVQRFF
DDEIKKMGVENSYFPMFVSRHKLEFSPEVAWVTHYGDSPLPEKIAIRPTS
ETIMYPAYAKWIRSHRDLPLKLNQWCSVVRWEFKQPTPFLRTREFLWQEG
HTAHATEEEAWELVLDILELYRRWYEECLAVPVIKGEKSEGEKFAGGKKT
TTVEAFIPENGRGIQAATSHLLGTNFAKMFEIEFEDEEGHKRLVHQTSWG
CTTRSLGVMIMTHGDDKGLVIPPRVASVQVVIIPILFKDENTGEILGKCR
ELKTMLEKADIRVRIDDRSNYTPGWKYNHWEVKGVPLRLELGPKDLAKGT
ARVVRRDTGEAYQISWADLAPKLLELMEGIQRSLFEKAKARLHEGIEKIS
TFDEVMPALNRKHLVLAPWCEDPESEEQIKKETQKLSEIQATGAMKTLCI
PFDQPPMPEGTKCFYTGKPAKRWTLWGRSY
3D structure
PDB5xiq Targeting Prolyl-tRNA Synthetase to Accelerate Drug Discovery against Malaria, Leishmaniasis, Toxoplasmosis, Cryptosporidiosis, and Coccidiosis
ChainB
Resolution2.19 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 ANP B R470 E472 R481 T482 F485 Q555 T558 T592 R594 R130 E132 R141 T142 F145 Q215 T218 T252 R254
BS02 HFG B F415 E418 P438 T439 E441 R470 F534 H560 F75 E78 P98 T99 E101 R130 F194 H220
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:5xiq, PDBe:5xiq, PDBj:5xiq
PDBsum5xiq
PubMed28867614
UniProtS8G8I1

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