Structure of PDB 4zyq Chain L

Receptor sequence
>4zyqL (length=511) Species: 186763 (Plasmodium falciparum FcB1/Columbia) [Search protein sequence]
SEVPQVVSLDPTSIPIEYNTPIHDIKVQVYDIKGGCNVEEGLTIFLVNNP
GKENGPVKISSKVNDKQVSEFLKDENMEKFNVKLGTSKHFYMFNDNKNSV
AVGYVGCGSVADLSEADMKRVVLSLVTMLHDNKLSKLTVVFEINVDKNLF
RFFLETLFYEYMTDERFKSEYIKHLGVYINNADTYKEEVEKARVYYFGTY
YASQLIAAPSNYCNPVSLSNAAVELAQKLNLEYKILGVKELEELKMGAYL
SVGKGSMYPNKFIHLTYKSKGDVKKKIALVGKGITFDSGGYNLKAAPGSM
IDLMKFDMSGCAAVLGCAYCVGTLKPENVEIHFLSAVCENMVSKNSYRPG
DIITASNGKTIEVGNTDAEGRLTLADALVYAEKLGVDYIVDIATLTGAML
YSLGTSYAGVFGNNEELINKILQSSKTSNEPVWWLPIINEYRATLNSKYA
DINQISSSVKASSIVASLFLKEFVQNTAWAHIDIAGVSWNFKARKPKGFG
VRLLTEFVLND
3D structure
PDB4zyq Potent dual inhibitors of Plasmodium falciparum M1 and M17 aminopeptidases through optimization of S1 pocket interactions.
ChainL
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) 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 4U6 L D379 K386 M392 D459 E461 L487 G489 L492 A577 D287 K294 M300 D367 E369 L395 G397 L400 A485
BS02 ZN L K374 D379 D399 E461 K282 D287 D307 E369
BS03 ZN L D379 D459 E461 D287 D367 E369
BS04 CO3 L A460 G462 R463 L487 A368 G370 R371 L395
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:4zyq, PDBe:4zyq, PDBj:4zyq
PDBsum4zyq
PubMed26807544
UniProtA0A024V0B1

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