Structure of PDB 2ef5 Chain B

Receptor sequence
>2ef5B (length=273) Species: 274 (Thermus thermophilus) [Search protein sequence]
ERVAVVGVPMDLGVDMGPSALRYARLLEQLEDLGYTVEDLGDVPVSLAYL
EEIRAAALVLKERLAALPEGVFPIVLGGDHSLSMGSVAGAARGRRVGVVW
VDAHADFNTPETSSGNVHGMPLAVLSGLGHPRLTEVFRAVDPKDVVLVGV
RSLDPGEKRLLKEAGVRVYTMHEVDRLGVARIAEEVLKHLQGLPLHVSLD
ADVLDPTLAPGVGTPVPGGLTYREAHLLMEILAESGRVQSLDLVEVNPIL
DERNRTAEMLVGLALSLLGKRIF
3D structure
PDB2ef5 Crystal structure of the arginase from thermus thermophilus
ChainB
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H97 D119 H121 D123 H136 D218 D220 E263
Catalytic site (residue number reindexed from 1) H80 D102 H104 D106 H118 D200 D202 E245
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 D119 H121 D218 D220 D102 H104 D200 D202
BS02 MN B H97 D119 D123 D218 H80 D102 D106 D200
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:0006525 arginine metabolic process
GO:0019547 arginine catabolic process to ornithine
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2ef5, PDBe:2ef5, PDBj:2ef5
PDBsum2ef5
PubMed
UniProtQ5SI78

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