Structure of PDB 4q3v Chain C

Receptor sequence
>4q3vC (length=339) Species: 6183 (Schistosoma mansoni) [Search protein sequence]
KPKLLYTSANFLGIPTNRGQPKIGTYQGPELIRKSNFFQLVAEDGIQLTD
CGDIIPVELNEAEDPQRFGMKWSRSFSLTTLRIAERVEELMKQSNKKSTP
LVIVGGDHSMATGTILGHAEAKPDLCVLWIDAHGDINTPLNSASGNMHGM
PLSFLVKELQDQIPWLDDFEGIKPCLNASNIAYIGLRDLDAHETHDIRKH
GIAYFTMLDVDRMGIEAVIKEALLAVNPRLEKAIHLSFDIDALDPLVAPS
TGTAVPGGLTLREGLRICEEVSATGKLSVVELAELNPLLGSQEDVLKTQS
SAVHILRACLGHCRSGHLPFKVRNLTDQGIMSRAAHMQT
3D structure
PDB4q3v Crystal Structure of Schistosoma mansoni Arginase, a Potential Drug Target for the Treatment of Schistosomiasis.
ChainC
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H131 D154 H156 D158 H171 D262 D264 E307
Catalytic site (residue number reindexed from 1) H108 D131 H133 D135 H148 D239 D241 E284
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 C D154 H156 D262 D264 D131 H133 D239 D241
BS02 MN C H131 D154 D158 D262 H108 D131 D135 D239
BS03 S2C C D154 H156 D158 N160 S167 H171 D213 D262 D264 T276 E307 D131 H133 D135 N137 S144 H148 D190 D239 D241 T253 E284
Gene Ontology
Molecular Function
GO:0004053 arginase activity
GO:0016787 hydrolase activity
GO:0016813 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
GO:0030145 manganese ion 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:0005634 nucleus
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:4q3v, PDBe:4q3v, PDBj:4q3v
PDBsum4q3v
PubMed25007099
UniProtQ6WVP6

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