Structure of PDB 3kr4 Chain J

Receptor sequence

>3kr4J (length=513) Species: 36329 (Plasmodium falciparum 3D7)

SEVPQVVSLDPTSIPIEYNTPIHDIKVQVYDIKGGCNVEEGLTIFLVNNP
GKENGPVKISSKVNDKQVSEFLKDENMEKFNVKLGTSKHFYMFNDNKNSV
AVGYVGCGSVADLSEADMKRVVLSLVTMLHDNKLSKLTVVFEINVDKNLF
RFFLETLFYEYMTDERFKSNMEYIKHLGVYINNADTYKEEVEKARVYYFG
TYYASQLIAAPSNYCNPVSLSNAAVELAQKLNLEYKILGVKELEELKMGA
YLSVGKGSMYPNKFIHLTYKSKGDVKKKIALVGKGITFDSGGYNLKAAPG
SMIDLMKFDMSGCAAVLGCAYCVGTLKPENVEIHFLSAVCENMVSKNSYR
PGDIITASNGKTIEVGNTDAEGRLTLADALVYAEKLGVDYIVDIATLTGA
MLYSLGTSYAGVFGNNEELINKILQSSKTSNEPVWWLPIINEYRATLNSK
YADINQISSSVKASSIVASLFLKEFVQNTAWAHIDIAGVSWNFKARKPKG
FGVRLLTEFVLND

3D structure

• PDB: 3kr4 Structure of the Plasmodium falciparum M17 aminopeptidase and significance for the design of drugs targeting the neutral exopeptidases
• Chain: J
• Resolution: 2.0 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	J	A460 G462 R463 L487	A370 G372 R373 L397
BS02	ZN	J	K374 D379 D399 E461	K284 D289 D309 E371
BS03	BES	J	K374 D379 M392 M396 F398 D399 D459 E461 R463 T486 L487 T488 G489 A577	K284 D289 M302 M306 F308 D309 D369 E371 R373 T396 L397 T398 G399 A487	MOAD: Ki=25nM
BS04	MG	J	D379 D459 E461	D289 D369 E371

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:3kr4, PDBe:3kr4, PDBj:3kr4
• PDBsum: 3kr4
• PubMed: 20133789
• UniProt: Q8IL11|AMPL_PLAF7 Leucine aminopeptidase (Gene Name=LAP)