Structure of PDB 3sl0 Chain A

Receptor sequence

>3sl0A (length=308) Species: 36329 (Plasmodium falciparum 3D7)

KNVSIIGSPLAAGQPLGGVQLACDDLRKLGLHNVIDVLGWKYEDIGNIDN
CYYDNIRNIKEIGIFSKNLFDTMSNELRKKNFVLNIGGDHGVAFSSILSS
LQMYQNLRVIWIDAHGDINIPETSPSGNYHGMTLAHTLGLFKKKVPYFEW
SENLTYLKPENTAIIGIRDIDAYEKIILKKCNINYYTIFDIEKNGIYNTI
CTALEKIDPNSNCPIHISLDIDSVDNVFAPGTGTVAKGGLNYREINLLMK
ILAETKRVVSMDLVEYNPSLDEVDKKVHGDSLPILDNATKTGKLCLELIA
RVLGYDIV

3D structure

• PDB: 3sl0 Binding of alpha , alpha-disubstituted amino acids to arginase suggests new avenues for inhibitor design.
• Chain: A
• Resolution: 1.997 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H193 D216 H218 D220 H233 D323 D325 E368
• Catalytic site (residue number reindexed from 1): H90 D113 H115 D117 H130 D220 D222 E265
• Enzyme Commision number: 3.5.3.1: arginase.

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	MN	A	D216 H218 D323 D325	D113 H115 D220 D222
BS02	MN	A	H193 D216 D220 D323	H90 D113 D117 D220
BS03	FB5	A	D216 H218 D220 N222 S229 H233 G234 D274 D323 D325	D113 H115 D117 N119 S126 H130 G131 D171 D220 D222	PDBbind-CN: -logKd/Ki=2.70,Ki=2mM

Gene Ontology

Molecular Function

• GO:0004053 arginase activity
• GO:0016787 hydrolase activity
• GO:0030145 manganese ion binding
• GO:0042802 identical protein binding
• GO:0046872 metal ion binding

Biological Process

• GO:0000050 urea cycle
• GO:0006525 arginine metabolic process
• GO:0019547 arginine catabolic process to ornithine

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:3sl0, PDBe:3sl0, PDBj:3sl0
• PDBsum: 3sl0
• PubMed: 21728378
• UniProt: Q8I384|ARGI_PLAF7 Arginase (Gene Name=ARG)