Structure of PDB 4zy2 Chain K

Receptor sequence
>4zy2K (length=512) Species: 186763 (Plasmodium falciparum FcB1/Columbia) [Search protein sequence]
SEVPQVVSLDPTSIPIEYNTPIHDIKVQVYDIKGGCNVEEGLTIFLVNNP
GKENGPVKISSKVNDKQVSEFLKDENMEKFNVKLGTSKHFYMFNDNKNSV
AVGYVGCGSVADLSEADMKRVVLSLVTMLHDNKLSKLTVVFEINVDKNLF
RFFLETLFYEYMTDERFKSTDEYIKHLGVYINNADTYKEEVEKARVYYFG
TYYASQLIAAPSNYCNPVSLSNAAVELAQKLNLEYKILGVKELEELKMGA
YLSVGKGSMYPNKFIHLTYKSKGDVKKKIALVGKGITFDSGGYNLKAAPG
SMIDLMKFDMSGCAAVLGCAYCVGTLKPENVEIHFLSAVCENMVSKNSYR
PGDIITASNGKTIEVGNTDAEGRLTLADALVYAEKLGVDYIVDIATLTGA
MLYSLGTSYAGVFGNNEELINKILQSSKTSNEPVWWLPIINEYRATLNSK
YADINQISSSVKASSIVASLFLKEFVQNTAWAHIDIAGVSWNFKARKPKG
FGVRLLTEFVLN
3D structure
PDB4zy2 Potent dual inhibitors of Plasmodium falciparum M1 and M17 aminopeptidases through optimization of S1 pocket interactions.
ChainK
Resolution2.1 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) K296 R373
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 ZN K K374 D379 D399 E461 K284 D289 D309 E371
BS02 CO3 K A460 G462 R463 L487 A370 G372 R373 L397
BS03 ZN K D379 D459 E461 D289 D369 E371
BS04 4TL K K374 D379 M392 D459 E461 L487 G489 L492 A577 F583 K284 D289 M302 D369 E371 L397 G399 L402 A487 F493 MOAD: Ki=0.06uM
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:4zy2, PDBe:4zy2, PDBj:4zy2
PDBsum4zy2
PubMed26807544
UniProtA0A0L7M119

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