Structure of PDB 3mmr Chain A

Receptor sequence
>3mmrA (length=308) Species: 36329 (Plasmodium falciparum 3D7) [Search protein sequence]
KNVSIIGSPLAAGQPLGGVQLACDDLRKLGLHNVIDVLGWKYEDIGNIDN
CYYDNIRNIKEIGIFSKNLFDTMSNELRKKNFVLNIGGDHGVAFSSILSS
LQMYQNLRVIWIDAHGDINIPETSPSGNYHGMTLAHTLGLFKKKVPYFEW
SENLTYLKPENTAIIGIRDIDAYEKIILKKCNINYYTIFDIEKNGIYNTI
CTALEKIDPNSNCPIHISLDIDSVDNVFAPGTGTVAKGGLNYREINLLMK
ILAETKRVVSMDLVEYNPSLDEVDKKVHGDSLPILDNATKTGKLCLELIA
RVLGYDIV
3D structure
PDB3mmr Crystal structure of arginase from Plasmodium falciparum and implications for L-arginine depletion in malarial infection .
ChainA
Resolution2.14 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 H193 D216 D220 D323 H90 D113 D117 D220
BS02 MN A D216 H218 D323 D325 D113 H115 D220 D222
BS03 ABH A D216 H218 D220 S229 H233 G234 D274 D323 E368 D113 H115 D117 S126 H130 G131 D171 D220 E265 MOAD: Kd=11uM
PDBbind-CN: -logKd/Ki=4.96,Kd=11uM
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3mmr, PDBe:3mmr, PDBj:3mmr
PDBsum3mmr
PubMed20527960
UniProtQ8I384|ARGI_PLAF7 Arginase (Gene Name=ARG)

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