Structure of PDB 4r7m Chain B

Receptor sequence

>4r7mB (length=512) Species: 36329 (Plasmodium falciparum 3D7)

SEVPQVVSLDPTSIPIEYNTPIHDIKVQVYDIKGGCNVEEGLTIFLVNNP
GKENGPVKISSKVNDKQVSEFLKDENMEKFNVKLGTSKHFYMFNDNKNSV
AVGYVGCGSVADLSEADMKRVVLSLVTMLHDNKLSKLTVVFEINVDKNLF
RFFLETLFYEYMTDERFKSTDKEYIKHLGVYINNADTYKEEVEKARVYYF
GTYYASQLIAAPSNYCNPVSLSNAAVELAQKLNLEYKILGVKELEELKMG
AYLSVGKGSMYPNKFIHLTYKSKGDVKKKIALVGKGITFDSGGYNLKAAP
GSMIDLMKFDMSGCAAVLGCAYCVGTLKPENVEIHFLSAVCENMVSKNSY
RPGDIITASNGKTIEVGNTDAEGRLTLADALVYAEKLGVDYIVDIATLTG
AMLYSLGTSYAGVFGNNEELINKILQSSKTSNEPVWWLPIINEYRATLNS
KYADINQISSSVKASSIVASLFLKEFVQNTAWAHIDIAGVSWNFKARKPK
GFGVRLLTEFVL

3D structure

• PDB: 4r7m Two-Pronged Attack: Dual Inhibition of Plasmodium falciparum M1 and M17 Metalloaminopeptidases by a Novel Series of Hydroxamic Acid-Based Inhibitors.
• Chain: B
• Resolution: 2.85 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	B	K374 D379 D399 E461	K285 D290 D310 E372
BS02	CO3	B	A460 G462 R463 L487	A371 G373 R374 L398
BS03	ZN	B	D379 D459 E461	D290 D370 E372
BS04	3MW	B	K374 D379 K386 N457 D459 E461 L487 T488 G489 L492 A577	K285 D290 K297 N368 D370 E372 L398 T399 G400 L403 A488	BindingDB: Ki=0.011000nM

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:4r7m, PDBe:4r7m, PDBj:4r7m
• PDBsum: 4r7m
• PubMed: 25299353
• UniProt: Q8IL11|AMPL_PLAF7 Leucine aminopeptidase (Gene Name=LAP)