Structure of PDB 4r76 Chain K

Receptor sequence

>4r76K (length=509) Species: 186763 (Plasmodium falciparum FcB1/Columbia)

SEVPQVVSLDPTSIPIEYNTPIHDIKVQVYDIKGGCNVEEGLTIFLVNNP
KENGPVKISSKVNDKQVSEFLKDENMEKFNVKLGTSKHFYMFNDNKNSVA
VGYVGCGSVADLSEADMKRVVLSLVTMLHDNKLSKLTVVFEINVDKNLFR
FFLETLFYEYMTDERFKSEYIKHLGVYINNADTYKEEVEKARVYYFGTYY
ASQLIAAPSNYCNPVSLSNAAVELAQKLNLEYKILGVKELEELKMGAYLS
VGKGSMYPNKFIHLTYKSKGDVKKKIALVGKGITFDSGGYNLKAAPGSMI
DLMKFDMSGCAAVLGCAYCVGTLKPENVEIHFLSAVCENMVSKNSYRPGD
IITASNGKTIEVGNTDAEGRLTLADALVYAEKLGVDYIVDIATLTGAMLY
SLGTSYAGVFGNNEELINKILQSSKTSNEPVWWLPIINEYRATLNSKYAD
INQISSSVKASSIVASLFLKEFVQNTAWAHIDIAGVSWNFKARKPKGFGV
RLLTEFVLN

3D structure

• PDB: 4r76 Two-Pronged Attack: Dual Inhibition of Plasmodium falciparum M1 and M17 Metalloaminopeptidases by a Novel Series of Hydroxamic Acid-Based Inhibitors.
• Chain: K
• Resolution: 2.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K386 R463
• Catalytic site (residue number reindexed from 1): K293 R370
• 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	K	K374 D379 D399 E461	K281 D286 D306 E368
BS02	CO3	K	A460 G462 R463 L487	A367 G369 R370 L394
BS03	ZN	K	D379 D459 E461	D286 D366 E368
BS04	R5X	K	K374 D379 D459 E461 L487 T488 G489	K281 D286 D366 E368 L394 T395 G396	MOAD: Ki=0.014uM BindingDB: Ki=0.014000nM

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:4r76, PDBe:4r76, PDBj:4r76
• PDBsum: 4r76
• PubMed: 25299353
• UniProt: Q8IL11|AMPL_PLAF7 Leucine aminopeptidase (Gene Name=LAP)