Structure of PDB 3kr5 Chain D

Receptor sequence

>3kr5D (length=513) Species: 36329 (Plasmodium falciparum 3D7)

ASEVPQVVSLDPTSIPIEYNTPIHDIKVQVYDIKGGCNVEEGLTIFLVNN
PGKENGPVKISSKVNDKQVSEFLKDENMEKFNVKLGTSKHFYMFNDNKNS
VAVGYVGCGSVADLSEADMKRVVLSLVTMLHDNKLSKLTVVFEINVDKNL
FRFFLETLFYEYMTDERFKSMEYIKHLGVYINNADTYKEEVEKARVYYFG
TYYASQLIAAPSNYCNPVSLSNAAVELAQKLNLEYKILGVKELEELKMGA
YLSVGKGSMYPNKFIHLTYKSKGDVKKKIALVGKGITFDSGGYNLKAAPG
SMIDLMKFDMSGCAAVLGCAYCVGTLKPENVEIHFLSAVCENMVSKNSYR
PGDIITASNGKTIEVGNTDAEGRLTLADALVYAEKLGVDYIVDIATLTGA
MLYSLGTSYAGVFGNNEELINKILQSSKTSNEPVWWLPIINEYRATLNSK
YADINQISSSVKASSIVASLFLKEFVQNTAWAHIDIAGVSWNFKARKPKG
FGVRLLTEFVLND

3D structure

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

Enzymatic activity

• Catalytic site (original residue number in PDB): K386 R463
• Catalytic site (residue number reindexed from 1): K296 R373
• 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	D	A460 E461 G462 R463 L487	A370 E371 G372 R373 L397
BS02	ZN	D	K374 D379 D399 E461	K284 D289 D309 E371
BS03	ZN	D	D379 D459 E461	D289 D369 E371
BS04	BEY	D	D379 K386 M396 D399 N457 D459 L487 T488 G489 L492 A577	D289 K296 M306 D309 N367 D369 L397 T398 G399 L402 A487

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)