Structure of PDB 4r6t Chain A

Receptor sequence

>4r6tA (length=514) Species: 36329 (Plasmodium falciparum 3D7)

ASEVPQVVSLDPTSIPIEYNTPIHDIKVQVYDIKGGCNVEEGLTIFLVNN
PGKENGPVKISSKVNDKQVSEFLKDENMEKFNVKLGTSKHFYMFNDNKNS
VAVGYVGCGSVADLSEADMKRVVLSLVTMLHDNKLSKLTVVFEINVDKNL
FRFFLETLFYEYMTDERFKSTDEYIKHLGVYINNADTYKEEVEKARVYYF
GTYYASQLIAAPSNYCNPVSLSNAAVELAQKLNLEYKILGVKELEELKMG
AYLSVGKGSMYPNKFIHLTYKSKGDVKKKIALVGKGITFDSGGYNLKAAP
GSMIDLMKFDMSGCAAVLGCAYCVGTLKPENVEIHFLSAVCENMVSKNSY
RPGDIITASNGKTIEVGNTDAEGRLTLADALVYAEKLGVDYIVDIATLTG
AMLYSLGTSYAGVFGNNEELINKILQSSKTSNEPVWWLPIINEYRATLNS
KYADINQISSSVKASSIVASLFLKEFVQNTAWAHIDIAGVSWNFKARKPK
GFGVRLLTEFVLND

3D structure

• PDB: 4r6t Two-Pronged Attack: Dual Inhibition of Plasmodium falciparum M1 and M17 Metalloaminopeptidases by a Novel Series of Hydroxamic Acid-Based Inhibitors.
• Chain: A
• Resolution: 2.6 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K386 R463
• Catalytic site (residue number reindexed from 1): K297 R374
• 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	ZN	A	K374 D379 D399 E461	K285 D290 D310 E372
BS02	CO3	A	A460 G462 R463 L487	A371 G373 R374 L398
BS03	ZN	A	D379 D459 E461	D290 D370 E372
BS04	R5T	A	K386 M392 D459 E461 L487 G489 A577	K297 M303 D370 E372 L398 G400 A488	PDBbind-CN: -logKd/Ki=7.52,Ki=0.03uM BindingDB: Ki=0.030000nM

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:4r6t, PDBe:4r6t, PDBj:4r6t
• PDBsum: 4r6t
• PubMed: 25299353
• UniProt: Q8IL11|AMPL_PLAF7 Leucine aminopeptidase (Gene Name=LAP)