Structure of PDB 4r7m Chain E

Receptor sequence

>4r7mE (length=510) Species: 36329 (Plasmodium falciparum 3D7)

SEVPQVVSLDPTSIPIEYNTPIHDIKVQVYDIKGGCNVEEGLTIFLVNNP
KENGPVKISSKVNDKQVSEFLKDENMEKFNVKLGTSKHFYMFNDNKNSVA
VGYVGCGSVADLSEADMKRVVLSLVTMLHDNKLSKLTVVFEINVDKNLFR
FFLETLFYEYMTDERFKSTEYIKHLGVYINNADTYKEEVEKARVYYFGTY
YASQLIAAPSNYCNPVSLSNAAVELAQKLNLEYKILGVKELEELKMGAYL
SVGKGSMYPNKFIHLTYKSKGDVKKKIALVGKGITFDSGGYNLKAAPGSM
IDLMKFDMSGCAAVLGCAYCVGTLKPENVEIHFLSAVCENMVSKNSYRPG
DIITASNGKTIEVGNTDAEGRLTLADALVYAEKLGVDYIVDIATLTGAML
YSLGTSYAGVFGNNEELINKILQSSKTSNEPVWWLPIINEYRATLNSKYA
DINQISSSVKASSIVASLFLKEFVQNTAWAHIDIAGVSWNFKARKPKGFG
VRLLTEFVLN

3D structure

• PDB: 4r7m Two-Pronged Attack: Dual Inhibition of Plasmodium falciparum M1 and M17 Metalloaminopeptidases by a Novel Series of Hydroxamic Acid-Based Inhibitors.
• Chain: E
• Resolution: 2.85 Å

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.
  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 D399 E461	K282 D307 E369
BS02	CO3	E	A460 G462 R463 L487	A368 G370 R371 L395
BS03	ZN	E	D379 D459 E461	D287 D367 E369
BS04	3MW	E	D379 K386 D399 D459 L487 T488 G489 L492 A577	D287 K294 D307 D367 L395 T396 G397 L400 A485	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

External links

• PDB: RCSB:4r7m, PDBe:4r7m, PDBj:4r7m
• PDBsum: 4r7m
• PubMed: 25299353
• UniProt: Q8IL11|AMPL_PLAF7 Leucine aminopeptidase (Gene Name=LAP)