Structure of PDB 4q3r Chain D

Receptor sequence
>4q3rD (length=314) Species: 6183 (Schistosoma mansoni) [Search protein sequence]
LLYTSANFLGIPTNRGQPKIGTYQGPELIRKSNFFQLVAEDGIQLTDCGD
IIPVELNEAEDPQRFGMKWSRSFSLTTLRIAERVEELMKSTPLVIVGGDH
SMATGTILGHAEAKPDLCVLWIDAHGDINTPLNSASGNMHGMPLSFLVKE
LQDQIPWLDDFEGIKPCLNASNIAYIGLRDLDAHETHDIRKHGIAYFTML
DVDRMGIEAVIKEALLAVNPRLEKAIHLSFDIDALDPLVAPSTGTAVPGG
LTLREGLRICEEVSATGKLSVVELAELNPLLGSQEDVLKTQSSAVHILRA
CLGHCRSGHLPFKV
3D structure
PDB4q3r Crystal Structure of Schistosoma mansoni Arginase, a Potential Drug Target for the Treatment of Schistosomiasis.
ChainD
Resolution2.169 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) H100 D123 H125 D127 H140 D231 D233 E276
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 H100 D123 D127 D231
BS02 MN D D154 H156 D262 D264 D123 H125 D231 D233
BS03 XA2 D D154 H156 D158 N160 S167 H171 G172 D211 D213 D262 D264 E307 D123 H125 D127 N129 S136 H140 G141 D180 D182 D231 D233 E276 MOAD: Kd=0.54uM
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:4q3r, PDBe:4q3r, PDBj:4q3r
PDBsum4q3r
PubMed25007099
UniProtQ6WVP6

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