Structure of PDB 4r7m Chain L

Receptor sequence
>4r7mL (length=509) Species: 36329 (Plasmodium falciparum 3D7) [Search protein sequence]
SEVPQVVSLDPTSIPIEYNTPIHDIKVQVYDIKGGCNVEEGLTIFLVNNP
GNGPVKISSKVNDKVSEFLKDENMEKFNVKLGTSKHFYMFNDNKNSVAVG
YVGCGSVADLSEADMKRVVLSLVTMLHDNKLSKLTVVFEINVDKNLFRFF
LETLFYEYMTDERFKSTEYIKHLGVYINNADTYKEEVEKARVYYFGTYYA
SQLIAAPSNYCNPVSLSNAAVELAQKLNLEYKILGVKELEELKMGAYLSV
GKGSMYPNKFIHLTYKSKGDVKKKIALVGKGITFDSGGYNLKAAPGSMID
LMKFDMSGCAAVLGCAYCVGTLKPENVEIHFLSAVCENMVSKNSYRPGDI
ITASNGKTIEVGNTDAEGRLTLADALVYAEKLGVDYIVDIATLTGAMLYS
LGTSYAGVFGNNEELINKILQSSKTSNEPVWWLPIINEYRATLNSKYADI
NQISSSVKASSIVASLFLKEFVQNTAWAHIDIAGVSWNFKARKPKGFGVR
LLTEFVLND
3D structure
PDB4r7m Two-Pronged Attack: Dual Inhibition of Plasmodium falciparum M1 and M17 Metalloaminopeptidases by a Novel Series of Hydroxamic Acid-Based Inhibitors.
ChainL
Resolution2.85 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) K292 R369
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 L K374 D379 D399 E461 K280 D285 D305 E367
BS02 CO3 L A460 G462 R463 L487 A366 G368 R369 L393
BS03 ZN L D379 D459 E461 D285 D365 E367
BS04 3MW L K374 D379 N457 D459 E461 L487 G489 L492 K280 D285 N363 D365 E367 L393 G395 L398 BindingDB: Ki=0.011000nM
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:4r7m, PDBe:4r7m, PDBj:4r7m
PDBsum4r7m
PubMed25299353
UniProtQ8IL11|AMPL_PLAF7 Leucine aminopeptidase (Gene Name=LAP)

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