Structure of PDB 5xii Chain D

Receptor sequence
>5xiiD (length=474) Species: 508771 (Toxoplasma gondii ME49) [Search protein sequence]
AMVTAKKDENFSEWYTQAIVRSEMIEYYDISGCYIMRPWAFHIWEKVQRF
FDDEIKKMGVENSYFPMFVSRHKLEKGFSPEVAWVTHYGDSPLPEKIAIR
PTSETIMYPAYAKWIRSHRDLPLKLNQWCSVVRWEFKQPTPFLRTREFLW
QEGHTAHATEEEAWELVLDILELYRRWYEECLAVPVIKGEKSEGEKFAGG
KKTTTVEAFIPENGRGIQAATSHLLGTNFAKMFEIEFEDEEGHKRLVHQT
SWGCTTRSLGVMIMTHGDDKGLVIPPRVASVQVVIIPTGEILGKCRELKT
MLEKADIRVRIDDRSNYTPGWKYNHWEVKGVPLRLELGPKDLAKGTARVV
RRDTGEAYQISWADLAPKLLELMEGIQRSLFEKAKARLHEGIEKISTFDE
VMPALNRKHLVLAPWCEDPESEEQIKKETQKLSEIQGAMKTLCIPFDQPP
MPEGTKCFYTGKPAKRWTLWGRSY
3D structure
PDB5xii Targeting Prolyl-tRNA Synthetase to Accelerate Drug Discovery against Malaria, Leishmaniasis, Toxoplasmosis, Cryptosporidiosis, and Coccidiosis
ChainD
Resolution2.17 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 D R470 E472 L480 R481 T482 F485 Q555 T558 T592 R594 R133 E135 L143 R144 T145 F148 Q218 T221 T255 R257
BS02 86X D F415 E418 V419 P438 T439 E441 R470 W487 F534 H560 F78 E81 V82 P101 T102 E104 R133 W150 F197 H223 MOAD: ic50=72nM
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5xii, PDBe:5xii, PDBj:5xii
PDBsum5xii
PubMed28867614
UniProtS8G8I1

[Back to BioLiP]