Structure of PDB 3kr4 Chain E

Receptor sequence

>3kr4E (length=510) Species: 36329 (Plasmodium falciparum 3D7)

SEVPQVVSLDPTSIPIEYNTPIHDIKVQVYDIKGGCNVEEGLTIFLVNNP
GKENGPVKISSKVNDKQVSEFLKDENMEKFNVKLGTSKHFYMFNDNKNSV
AVGYVGCGSVADLSEADMKRVVLSLVTMLHDNKLSKLTVVFEINVDKNLF
RFFLETLFYEYMTDERFKSEYIKHLGVYINNADTYKEEVEKARVYYFGTY
YASQLIAAPSNYCNPVSLSNAAVELAQKLNLEYKILGVKELEELKMGAYL
SVGKGSMYPNKFIHLTYKSKGDVKKKIALVGKGITFDSGGYNLKAAPGSM
IDLMKFDMSGCAAVLGCAYCVGTLKPENVEIHFLSAVCENMVSKNSYRPG
DIITASNGKTIEVGNTDAEGRLTLADALVYAEKLGVDYIVDIATLTGAML
YSLGTSYAGVFGNNEELINKILQSSKTSNEPVWWLPIINEYRATLNSKYA
DINQISSSVKASSIVASLFLKEFVQNTAWAHIDIAGVSWNFKARKPKGFG
VRLLTEFVLN

3D structure

• PDB: 3kr4 Structure of the Plasmodium falciparum M17 aminopeptidase and significance for the design of drugs targeting the neutral exopeptidases
• Chain: E
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K386 R463
• Catalytic site (residue number reindexed from 1): K294 R371
• 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	E	A460 G462 R463 L487	A368 G370 R371 L395
BS02	ZN	E	K374 D379 D399 E461	K282 D287 D307 E369
BS03	BES	E	K374 D379 M392 M396 F398 D399 D459 E461 R463 T486 L487 T488	K282 D287 M300 M304 F306 D307 D367 E369 R371 T394 L395 T396	MOAD: Ki=25nM
BS04	MG	E	D379 D459 E461	D287 D367 E369

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)