Structure of PDB 3kr5 Chain G

Receptor sequence

>3kr5G (length=516) Species: 36329 (Plasmodium falciparum 3D7)

SEVPQVVSLDPTSIPIEYNTPIHDIKVQVYDIKGGCNVEEGLTIFLVNNP
GKENGPVKISSKVNDKQVSEFLKDENMEKFNVKLGTSKHFYMFNDNKNSV
AVGYVGCGSVADLSEADMKRVVLSLVTMLHDNKLSKLTVVFEINVDKNLF
RFFLETLFYEYMTDERFKSTDKNMEYIKHLGVYINNADTYKEEVEKARVY
YFGTYYASQLIAAPSNYCNPVSLSNAAVELAQKLNLEYKILGVKELEELK
MGAYLSVGKGSMYPNKFIHLTYKSKGDVKKKIALVGKGITFDSGGYNLKA
APGSMIDLMKFDMSGCAAVLGCAYCVGTLKPENVEIHFLSAVCENMVSKN
SYRPGDIITASNGKTIEVGNTDAEGRLTLADALVYAEKLGVDYIVDIATL
TGAMLYSLGTSYAGVFGNNEELINKILQSSKTSNEPVWWLPIINEYRATL
NSKYADINQISSSVKASSIVASLFLKEFVQNTAWAHIDIAGVSWNFKARK
PKGFGVRLLTEFVLND

3D structure

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

Enzymatic activity

• Catalytic site (original residue number in PDB): K386 R463
• Catalytic site (residue number reindexed from 1): K299 R376
• 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	G	A460 G462 R463 L487	A373 G375 R376 L400
BS02	ZN	G	K374 D379 D399 E461	K287 D292 D312 E374
BS03	ZN	G	D379 D459 E461	D292 D372 E374
BS04	BEY	G	K374 K386 M392 M396 F398 D399 N457 D459 L487 G489 L492 A577	K287 K299 M305 M309 F311 D312 N370 D372 L400 G402 L405 A490

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)