Structure of PDB 6eee Chain H

Receptor sequence

>6eeeH (length=513) Species: 137071 (Plasmodium falciparum HB3)

SEVPQVVSLDPTSIPIEYNTPIHDIKVQVYDIKGGCNVEEGLTIFLVNNP
KENGPVKISSKVNDKQVSEFLKDENMEKFNVKLGTSKHFYMFNDNKNSVA
VGYVGCGSVADLSEADMKRVVLSLVTMLHDNKLSKLTVVFEINVDKNLFR
FFLETLFYEYMTDERFKSTDMEYIKHLGVYINNADTYKEEVEKARVYYFG
TYYASQLIAAPSNYCNPVSLSNAAVELAQKLNLEYKILGVKELEELKMGA
YLSVGKGSMYPNKFIHLTYKSKGDVKKKIALVGKGITFDSGGYNLKAAPG
SMIDLMKFDMSGCAAVLGCAYCVGTLKPENVEIHFLSAVCENMVSKNSYR
PGDIITASNGKTIEVGNTDAEGRLTLADALVYAEKLGVDYIVDIATLTGA
MLYSLGTSYAGVFGNNEELINKILQSSKTSNEPVWWLPIINEYRATLNSK
YADINQISSSVKASSIVASLFLKEFVQNTAWAHIDIAGVSWNFKARKPKG
FGVRLLTEFVLND

3D structure

• PDB: 6eee Hydroxamic Acid Inhibitors Provide Cross-Species Inhibition of Plasmodium M1 and M17 Aminopeptidases.
• Chain: H
• Resolution: 2.3 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.

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	J4V	H	K374 D379 M392 N457 D459 E461 L487 G489 L492 S554 A577	K284 D289 M302 N367 D369 E371 L397 G399 L402 S464 A487	MOAD: Ki=28.9nM
BS02	CO3	H	A460 G462 R463 L487	A370 G372 R373 L397
BS03	ZN	H	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:6eee, PDBe:6eee, PDBj:6eee
• PDBsum: 6eee
• PubMed: 30537832
• UniProt: A0A0L7KHE6