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Structure of PDB 2cev Chain F

Receptor sequence >2cevF (length=298) Species: 33931 ([Bacillus] caldovelox) [Search protein sequence] KPISIIGVPMDLGQTRRGVDMGPSAMRYAGVIERLERLHYDIEDLGDIPI GKAERLHEQGDSRLRNLKAVAEANEKLAAAVDQVVQRGRFPLVLGGDHSI AIGTLAGVAKHYERLGVIWYDAHGDVNTAETSPSGNIHGMPLAASLGFGH PALTQIGGYSPKIKPEHVVLIGVRSLDEGEKKFIREKGIKIYTMHEVDRL GMTRVMEETIAYLKERTDGVHLSLDLDGLDPSDAPGVGTPVIGGLTYRES HLAMEMLAEAQIITSAEFVEVNPILDERNKTASVAVALMGSLFGEKLM

3D structure PDB 2cev Crystal structures of Bacillus caldovelox arginase in complex with substrate and inhibitors reveal new insights into activation, inhibition and catalysis in the arginase superfamily. Chain F Resolution 2.15 Å 3D structure Catalytic site residues are labeled in the structure [Spin on] [Spin off] [Reset orientation] [High quality] [Low quality] [White background] [Black background] [Download] [Download structure with residue number starting from 1]

Enzymatic activity Catalytic site (original residue number in PDB) H99 D122 H124 D126 H139 D226 D228 E271 Catalytic site (residue number reindexed from 1) H98 D121 H123 D125 H138 D225 D227 E270 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 F H99 D122 D126 D226 H98 D121 D125 D225 BS02 MN F D122 H124 D226 D228 D121 H123 D225 D227 BS03 GAI F H252 E256 H251 E255

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:0005737	cytoplasm

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