Structure of PDB 3kr5 Chain A

Receptor sequence

>3kr5A (length=518) Species: 36329 (Plasmodium falciparum 3D7)

ASEVPQVVSLDPTSIPIEYNTPIHDIKVQVYDIKGGCNVEEGLTIFLVNN
PGKENGPVKISSKVNDKQVSEFLKDENMEKFNVKLGTSKHFYMFNDNKNS
VAVGYVGCGSVADLSEADMKRVVLSLVTMLHDNKLSKLTVVFEINVDKNL
FRFFLETLFYEYMTDERFKSTDKNVMEYIKHLGVYINNADTYKEEVEKAR
VYYFGTYYASQLIAAPSNYCNPVSLSNAAVELAQKLNLEYKILGVKELEE
LKMGAYLSVGKGSMYPNKFIHLTYKSKGDVKKKIALVGKGITFDSGGYNL
KAAPGSMIDLMKFDMSGCAAVLGCAYCVGTLKPENVEIHFLSAVCENMVS
KNSYRPGDIITASNGKTIEVGNTDAEGRLTLADALVYAEKLGVDYIVDIA
TLTGAMLYSLGTSYAGVFGNNEELINKILQSSKTSNEPVWWLPIINEYRA
TLNSKYADINQISSSVKASSIVASLFLKEFVQNTAWAHIDIAGVSWNFKA
RKPKGFGVRLLTEFVLND

3D structure

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

Enzymatic activity

• Catalytic site (original residue number in PDB): K386 R463
• Catalytic site (residue number reindexed from 1): K301 R378
• 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	A	A460 G462 R463 L487	A375 G377 R378 L402
BS02	ZN	A	D379 D459 E461	D294 D374 E376
BS03	ZN	A	K374 D379 D399 E461	K289 D294 D314 E376
BS04	BEY	A	K374 D379 K386 M396 F398 D399 N457 D459 E461 L487 T488 G489 A577	K289 D294 K301 M311 F313 D314 N372 D374 E376 L402 T403 G404 A492	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)