Structure of PDB 4wi1 Chain A

Receptor sequence
>4wi1A (length=440) Species: 36329 (Plasmodium falciparum 3D7) [Search protein sequence]
AHHHHHHSNILGITSKKIENFSDWYTQVIVKSELIEYYGCYILRPAAYYI
WECVQAFFNKEIKKLNVENSYFPLFVTSETIMYSVFPKWIRSYRDLPLKL
NQWNTVREFLWQEGHTAHKNEEEAVKLVFDILDLYRRWYEEYLAVPIIKG
IKSEGEKFGGANFTSTAEAFISENGRAIQAATSHYLGTNFAKMFKIEFED
ENEVKQYVHQTSWGCTTRSIGIMIMTHGDDKGLVLPPNVSKYKVVIVPIF
YKTTDENAIHSYCKDIEKILKNAQINCVYDDRASYSPGYKFNHWELRGIP
IRIEVGPKDLQNNSCVIVRRDNNEKCNVKKESVLLETQQMLVDIHKNLFL
KAKKKLDDSIVQVTSFSEVMNALNKKKMVLAPWCEDIATEEEIKKETQRL
SSGAMKPLCIPLDQPPMPPNMKCFWSGKPAKRWCLFGRSY
3D structure
PDB4wi1 Biochemical and Structural Characterization of Selective Allosteric Inhibitors of the Plasmodium falciparum Drug Target, Prolyl-tRNA-synthetase.
ChainA
Resolution1.65 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 3O6 A Y266 A291 R403 E404 I474 T513 I516 G517 M521 Y25 A47 R107 E108 I178 T217 I220 G221 M225 MOAD: ic50=5uM
PDBbind-CN: -logKd/Ki=5.30,IC50=5uM
BS02 MG A T362 Q384 E409 T80 Q102 E113
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:4wi1, PDBe:4wi1, PDBj:4wi1
PDBsum4wi1
PubMed27798837
UniProtQ8I5R7|SYP_PLAF7 Proline--tRNA ligase (Gene Name=proRS)

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