Structure of PDB 3kr5 Chain L

Receptor sequence
>3kr5L (length=513) Species: 36329 (Plasmodium falciparum 3D7) [Search protein sequence]
SEVPQVVSLDPTSIPIEYNTPIHDIKVQVYDIKGGCNVEEGLTIFLVNNP
GKENGPVKISSKVNDKQVSEFLKDENMEKFNVKLGTSKHFYMFNDNKNSV
AVGYVGCGSVADLSEADMKRVVLSLVTMLHDNKLSKLTVVFEINVDKNLF
RFFLETLFYEYMTDERFKSEYIKHLGVYINNADTYKEEVEKARVYYFGTY
YASQLIAAPSNYCNPVSLSNAAVELAQKLNLEYKILGVKELEELKMGAYL
SVGKGSMYPNKFIHLTYKSKGDVKKKIALVGKGITFDSGGYNLKAAPGSM
IDLMKFDMSGCAAVLGCAYCVGTLKPENVEIHFLSAVCENMVSKNSYRPG
DIITASNGKTIEVGNTDAEGRLTLADALVYAEKLGVDYIVDIATLTGAML
YSLGTSYAGVFGNNEELINKILQSSKTSNEPVWWLPIINEYRATLNSKYA
DINQISSSVKASSIVASLFLKEFVQNTAWAHIDIAGVSWNFKARKPKGFG
VRLLTEFVLNDAL
3D structure
PDB3kr5 Structure of the Plasmodium falciparum M17 aminopeptidase and significance for the design of drugs targeting the neutral exopeptidases
ChainL
Resolution2.56 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K386 R463
Catalytic site (residue number reindexed from 1) K294 R371
Enzyme Commision number 3.4.11.1: leucyl aminopeptidase.
3.4.13.-
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 CO3 L A460 E461 G462 R463 L487 A368 E369 G370 R371 L395
BS02 ZN L K374 D399 E461 K282 D307 E369
BS03 ZN L D379 D459 E461 D287 D367 E369
BS04 BEY L D379 K386 M396 F398 D399 N457 D459 L487 G489 L492 A577 D287 K294 M304 F306 D307 N365 D367 L395 G397 L400 A485
Gene Ontology
Molecular Function
GO:0030145 manganese ion binding
GO:0046872 metal ion binding
GO:0070006 metalloaminopeptidase activity
Biological Process
GO:0006508 proteolysis
GO:0019538 protein metabolic process
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:3kr5, PDBe:3kr5, PDBj:3kr5
PDBsum3kr5
PubMed20133789
UniProtQ8IL11|AMPL_PLAF7 Leucine aminopeptidase (Gene Name=LAP)

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