Structure of PDB 6eee Chain E

Receptor sequence
>6eeeE (length=510) Species: 137071 (Plasmodium falciparum HB3) [Search protein sequence]
SEVPQVVSLDPTSIPIEYNTPIHDIKVQVYDIKGGCNVEEGLTIFLVNNP
GKENGPVKISSKVNDKQVSEFLKDENMEKFNVKLGTSKHFYMFNDNKNSV
AVGYVGCGSVADLSEADMKRVVLSLVTMLHDNKLSKLTVVFEINVDKNLF
RFFLETLFYEYMTDERFKSEYIKHLGVYINNADTYKEEVEKARVYYFGTY
YASQLIAAPSNYCNPVSLSNAAVELAQKLNLEYKILGVKELEELKMGAYL
SVGKGSMYPNKFIHLTYKSKGDVKKKIALVGKGITFDSGGYNLKAAPGSM
IDLMKFDMSGCAAVLGCAYCVGTLKPENVEIHFLSAVCENMVSKNSYRPG
DIITASNGKTIEVGNTDAEGRLTLADALVYAEKLGVDYIVDIATLTGAML
YSLGTSYAGVFGNNEELINKILQSSKTSNEPVWWLPIINEYRATLNSKYA
DINQISSSVKASSIVASLFLKEFVQNTAWAHIDIAGVSWNFKARKPKGFG
VRLLTEFVLN
3D structure
PDB6eee Hydroxamic Acid Inhibitors Provide Cross-Species Inhibition of Plasmodium M1 and M17 Aminopeptidases.
ChainE
Resolution2.3 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.
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 J4V E K374 D379 M392 D459 E461 L487 T488 G489 L492 S554 K282 D287 M300 D367 E369 L395 T396 G397 L400 S462 MOAD: Ki=28.9nM
BS02 CO3 E A460 G462 R463 L487 A368 G370 R371 L395
BS03 ZN E D379 D459 E461 D287 D367 E369
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:6eee, PDBe:6eee, PDBj:6eee
PDBsum6eee
PubMed30537832
UniProtA0A0L7KHE6

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