Structure of PDB 4q3q Chain B

Receptor sequence
>4q3qB (length=335) Species: 6183 (Schistosoma mansoni) [Search protein sequence]
KLLYTSANFLGIPTNRGQPKIGTYQGPELIRKSNFFQLVAEDGIQLTDCG
DIIPVELNEAEDPQRFGMKWSRSFSLTTLRIAERVEELMKQSNKSTPLVI
VGGDHSMATGTILGHAEAKPDLCVLWIDAHGDINTPLNSASGNMHGMPLS
FLVKELQDQIPWLDDFEGIKPCLNASNIAYIGLRDLDAHETHDIRKHGIA
YFTMLDVDRMGIEAVIKEALLAVNPRLEKAIHLSFDIDALDPLVAPSTGT
AVPGGLTLREGLRICEEVSATGKLSVVELAELNPLLGSQEDVLKTQSSAV
HILRACLGHCRSGHLPFKVRNLTDQGIMSRAAHMQ
3D structure
PDB4q3q Crystal Structure of Schistosoma mansoni Arginase, a Potential Drug Target for the Treatment of Schistosomiasis.
ChainB
Resolution2.001 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) H105 D128 H130 D132 H145 D236 D238 E281
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 H105 D128 D132 D236
BS02 MN B D154 H156 D262 D264 D128 H130 D236 D238
BS03 ABH B D154 H156 D158 S167 H171 D213 D262 E307 D128 H130 D132 S141 H145 D187 D236 E281 MOAD: Kd=1.3uM
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:4q3q, PDBe:4q3q, PDBj:4q3q
PDBsum4q3q
PubMed25007099
UniProtQ6WVP6

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