Structure of PDB 4q3t Chain B

Receptor sequence
>4q3tB (length=335) Species: 6183 (Schistosoma mansoni) [Search protein sequence]
PKLLYTSANFLGIPTNRGQPKIGTYQGPELIRKSNFFQLVAEDGIQLTDC
GDIIPVELNEAEDPQRFGMKWSRSFSLTTLRIAERVEELMKQSSTPLVIV
GGDHSMATGTILGHAEAKPDLCVLWIDAHGDINTPLNSASGNMHGMPLSF
LVKELQDQIPWLDDFEGIKPCLNASNIAYIGLRDLDAHETHDIRKHGIAY
FTMLDVDRMGIEAVIKEALLAVNPRLEKAIHLSFDIDALDPLVAPSTGTA
VPGGLTLREGLRICEEVSATGKLSVVELAELNPLLGSQEDVLKTQSSAVH
ILRACLGHCRSGHLPFKVRNLTDQGIMSRAAHMQT
3D structure
PDB4q3t Crystal Structure of Schistosoma mansoni Arginase, a Potential Drug Target for the Treatment of Schistosomiasis.
ChainB
Resolution2.142 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) H104 D127 H129 D131 H144 D235 D237 E280
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 B H131 D154 D158 D262 H104 D127 D131 D235
BS02 MN B D154 H156 D262 D264 D127 H129 D235 D237
BS03 HAR B D154 H156 D158 N160 H171 G172 D213 D262 E307 D127 H129 D131 N133 H144 G145 D186 D235 E280 MOAD: Kd=0.33uM
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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Cellular Component
External links
PDB RCSB:4q3t, PDBe:4q3t, PDBj:4q3t
PDBsum4q3t
PubMed25007099
UniProtQ6WVP6

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