Structure of PDB 4r6t Chain E

Receptor sequence
>4r6tE (length=513) Species: 36329 (Plasmodium falciparum 3D7) [Search protein sequence]
SEVPQVVSLDPTSIPIEYNTPIHDIKVQVYDIKGGCNVEEGLTIFLVNNP
KENGPVKISSKVNDKQVSEFLKDENMEKFNVKLGTSKHFYMFNDNKNSVA
VGYVGCGSVADLSEADMKRVVLSLVTMLHDNKLSKLTVVFEINVDKNLFR
FFLETLFYEYMTDERFKSTVNMEYIKHLGVYINNADTYKEEVEKARVYYF
GTYYASQLIAAPSNYCNPVSLSNAAVELAQKLNLEYKILGVKELEELKMG
AYLSVGKGSMYPNKFIHLTYKSKGDVKKKIALVGKGITFDSGGYNLKAAP
GSMIDLMKFDMSGCAAVLGCAYCVGTLKPENVEIHFLSAVCENMVSKNSY
RPGDIITASNGKTIEVGNTDAEGRLTLADALVYAEKLGVDYIVDIATLTG
AMLYSLGTSYAGVFGNNEELINKILQSSKTSNEPVWWLPIINEYRATLNS
KYADINQISSSVKASSIVASLFLKEFVQNTAWAHIDIAGVSWNFKARKPK
GFGVRLLTEFVLN
3D structure
PDB4r6t Two-Pronged Attack: Dual Inhibition of Plasmodium falciparum M1 and M17 Metalloaminopeptidases by a Novel Series of Hydroxamic Acid-Based Inhibitors.
ChainE
Resolution2.6 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) K297 R374
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 ZN E K374 D379 D399 E461 K285 D290 D310 E372
BS02 CO3 E A460 G462 R463 L487 A371 G373 R374 L398
BS03 ZN E D379 D459 E461 D290 D370 E372
BS04 R5T E D379 K386 D459 E461 L487 T488 G489 S554 D290 K297 D370 E372 L398 T399 G400 S465 BindingDB: Ki=0.030000nM
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:4r6t, PDBe:4r6t, PDBj:4r6t
PDBsum4r6t
PubMed25299353
UniProtQ8IL11|AMPL_PLAF7 Leucine aminopeptidase (Gene Name=LAP)

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