Structure of PDB 4q3v Chain A

Receptor sequence
>4q3vA (length=337) Species: 6183 (Schistosoma mansoni) [Search protein sequence]
PKLLYTSANFLGIPTNRGQPKIGTYQGPELIRKSNFFQLVAEDGIQLTDC
GDIIPVELNEAEDPQRFGMKWSRSFSLTTLRIAERVEELMKQSNKSTPLV
IVGGDHSMATGTILGHAEAKPDLCVLWIDAHGDINTPLNSASGNMHGMPL
SFLVKELQDQIPWLDDFEGIKPCLNASNIAYIGLRDLDAHETHDIRKHGI
AYFTMLDVDRMGIEAVIKEALLAVNPRLEKAIHLSFDIDALDPLVAPSTG
TAVPGGLTLREGLRICEEVSATGKLSVVELAELNPLLGSQEDVLKTQSSA
VHILRACLGHCRSGHLPFKVRNLTDQGIMSRAAHMQT
3D structure
PDB4q3v Crystal Structure of Schistosoma mansoni Arginase, a Potential Drug Target for the Treatment of Schistosomiasis.
ChainA
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) H106 D129 H131 D133 H146 D237 D239 E282
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 H131 D154 D158 D262 H106 D129 D133 D237
BS02 MN A D154 H156 D262 D264 D129 H131 D237 D239
BS03 S2C A D154 H156 D158 N160 S167 H171 D213 D262 D264 E307 D129 H131 D133 N135 S142 H146 D188 D237 D239 E282
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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