Structure of PDB 4r7m Chain I

Receptor sequence

>4r7mI (length=516) Species: 36329 (Plasmodium falciparum 3D7)

SEVPQVVSLDPTSIPIEYNTPIHDIKVQVYDIKGGCNVEEGLTIFLVNNP
GKENGPVKISSKVNDKQVSEFLKDENMEKFNVKLGTSKHFYMFNDNKNSV
AVGYVGCGSVADLSEADMKRVVLSLVTMLHDNKLSKLTVVFEINVDKNLF
RFFLETLFYEYMTDERFKSTDKNMEYIKHLGVYINNADTYKEEVEKARVY
YFGTYYASQLIAAPSNYCNPVSLSNAAVELAQKLNLEYKILGVKELEELK
MGAYLSVGKGSMYPNKFIHLTYKSKGDVKKKIALVGKGITFDSGGYNLKA
APGSMIDLMKFDMSGCAAVLGCAYCVGTLKPENVEIHFLSAVCENMVSKN
SYRPGDIITASNGKTIEVGNTDAEGRLTLADALVYAEKLGVDYIVDIATL
TGAMLYSLGTSYAGVFGNNEELINKILQSSKTSNEPVWWLPIINEYRATL
NSKYADINQISSSVKASSIVASLFLKEFVQNTAWAHIDIAGVSWNFKARK
PKGFGVRLLTEFVLND

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: I
• Resolution: 2.85 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K386 R463
• Catalytic site (residue number reindexed from 1): K299 R376
• 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	I	K374 D379 D399	K287 D292 D312
BS02	CO3	I	A460 E461 G462 R463 L487	A373 E374 G375 R376 L400
BS03	ZN	I	D379 D459 E461	D292 D372 E374
BS04	3MW	I	K374 D379 F398 D459 E461 L487 T488 G489 S554	K287 D292 F311 D372 E374 L400 T401 G402 S467	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)