Structure of PDB 4q3s Chain D

Receptor sequence
>4q3sD (length=331) Species: 6183 (Schistosoma mansoni) [Search protein sequence]
LLYTSANFLGIPTNRGQPKIGTYQGPELIRKSNFFQLVAEDGIQLTDCGD
IIPVELNEAEDPQRFGMKWSRSFSLTTLRIAERVEELMKQSSTPLVIVGG
DHSMATGTILGHAEAKPDLCVLWIDAHGDINTPLNSASGNMHGMPLSFLV
KELQDQIPWLDDFEGIKPCLNASNIAYIGLRDLDAHETHDIRKHGIAYFT
MLDVDRMGIEAVIKEALLAVNPRLEKAIHLSFDIDALDPLVAPSTGTAVP
GGLTLREGLRICEEVSATGKLSVVELAELNPLLGSQEDVLKTQSSAVHIL
RACLGHCRSGHLPFKVRNLTDQGIMSRAAHM
3D structure
PDB4q3s Crystal Structure of Schistosoma mansoni Arginase, a Potential Drug Target for the Treatment of Schistosomiasis.
ChainD
Resolution2.11 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) H102 D125 H127 D129 H142 D233 D235 E278
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 D H131 D154 D158 D262 H102 D125 D129 D233
BS02 MN D D154 H156 D262 D264 D125 H127 D233 D235
BS03 X7A D D154 H156 D158 S167 H171 D211 D213 D262 E307 D125 H127 D129 S138 H142 D182 D184 D233 E278 MOAD: Kd=0.26uM
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:4q3s, PDBe:4q3s, PDBj:4q3s
PDBsum4q3s
PubMed25007099
UniProtQ6WVP6

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