Structure of PDB 4o0h Chain B

Receptor sequence
>4o0hB (length=295) Species: 9606 (Homo sapiens) [Search protein sequence]
HMNPIVVVHGGGAGPISKDRKERVHQGMVRAATVGYGILREGGSAVDAVE
GAVVALEDDPEFNAGCGSVLNTNGEVEMDASIMDGKDLSAGAVSAVQCIA
NPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVTERNKKRLE
KEKHTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDI
GAVSTTGHGESILKVNLARLTLFHIEQGKTVEEAADLSLGYMKSRVKGLG
GLIVVSKTGDWVAKWTSTSMPWAAAKDGKLHFGIDPDDTTITDLP
3D structure
PDB4o0h Elucidation of the Specific Function of the Conserved Threonine Triad Responsible for Human l-Asparaginase Autocleavage and Substrate Hydrolysis.
ChainB
Resolution1.97 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N62 T168 T186 R196 T219 G220
Catalytic site (residue number reindexed from 1) N63 T155 T173 R183 T206 G207
Enzyme Commision number 3.4.19.5: beta-aspartyl-peptidase.
3.5.1.1: asparaginase.
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 IAS B T168 R196 D199 T219 G220 G222 T155 R183 D186 T206 G207 G209
Gene Ontology
Molecular Function
GO:0003948 N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity
GO:0004067 asparaginase activity
GO:0008233 peptidase activity
GO:0008798 beta-aspartyl-peptidase activity
GO:0016787 hydrolase activity
Biological Process
GO:0006508 proteolysis
GO:0033345 asparagine catabolic process via L-aspartate
Cellular Component
GO:0001917 photoreceptor inner segment
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005829 cytosol

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Biological Process
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Cellular Component
External links
PDB RCSB:4o0h, PDBe:4o0h, PDBj:4o0h
PDBsum4o0h
PubMed24768817
UniProtQ7L266|ASGL1_HUMAN Isoaspartyl peptidase/L-asparaginase (Gene Name=ASRGL1)

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