Structure of PDB 3kr5 Chain F

Receptor sequence

>3kr5F (length=510) Species: 36329 (Plasmodium falciparum 3D7)

SEVPQVVSLDPTSIPIEYNTPIHDIKVQVYDIKGGCNVEEGLTIFLVNNP
KENGPVKISSKVNDKQVSEFLKDENMEKFNVKLGTSKHFYMFNDNKNSVA
VGYVGCGSVADLSEADMKRVVLSLVTMLHDNKLSKLTVVFEINVDKNLFR
FFLETLFYEYMTDERFKSEYIKHLGVYINNADTYKEEVEKARVYYFGTYY
ASQLIAAPSNYCNPVSLSNAAVELAQKLNLEYKILGVKELEELKMGAYLS
VGKGSMYPNKFIHLTYKSKGDVKKKIALVGKGITFDSGGYNLKAAPGSMI
DLMKFDMSGCAAVLGCAYCVGTLKPENVEIHFLSAVCENMVSKNSYRPGD
IITASNGKTIEVGNTDAEGRLTLADALVYAEKLGVDYIVDIATLTGAMLY
SLGTSYAGVFGNNEELINKILQSSKTSNEPVWWLPIINEYRATLNSKYAD
INQISSSVKASSIVASLFLKEFVQNTAWAHIDIAGVSWNFKARKPKGFGV
RLLTEFVLND

3D structure

• PDB: 3kr5 Structure of the Plasmodium falciparum M17 aminopeptidase and significance for the design of drugs targeting the neutral exopeptidases
• Chain: F
• Resolution: 2.56 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K386 R463
• Catalytic site (residue number reindexed from 1): K293 R370
• 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	CO3	F	A460 E461 G462 R463 L487	A367 E368 G369 R370 L394
BS02	ZN	F	K374 D379 D399 E461	K281 D286 D306 E368
BS03	ZN	F	D379 D459 E461	D286 D366 E368
BS04	BEY	F	K374 D379 K386 M396 F398 D399 N457 D459 A460 E461 L487 T488 G489 L492 A577	K281 D286 K293 M303 F305 D306 N364 D366 A367 E368 L394 T395 G396 L399 A484	PDBbind-CN: -logKd/Ki=7.89,Ki=13nM

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:3kr5, PDBe:3kr5, PDBj:3kr5
• PDBsum: 3kr5
• PubMed: 20133789
• UniProt: Q8IL11|AMPL_PLAF7 Leucine aminopeptidase (Gene Name=LAP)