Structure of PDB 4o0f Chain A

Receptor sequence
>4o0fA (length=296) Species: 9606 (Homo sapiens) [Search protein sequence]
HMNPIVVVHGGGAGPISKDRKERVHQGMVRAATVGYGILREGGSAVDAVE
GAVVALEDDPEFNAGCGSVLNTNGEVEMDASIMDGKDLSAGAVSAVQCIA
NPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVTERNKKRLE
KEKLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADND
IGAVSTAGHGESILKVNLARLTLFHIEQGKTVEEAADLSLGYMKSRVKGL
GGLIVVSKTGDWVAKWTSTSMPWAAAKDGKLHFGIDPDDTTITDLP
3D structure
PDB4o0f Elucidation of the Specific Function of the Conserved Threonine Triad Responsible for Human l-Asparaginase Autocleavage and Substrate Hydrolysis.
ChainA
Resolution1.92 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 A219 G220
Catalytic site (residue number reindexed from 1) N63 T156 T174 R184 A207 G208
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 GLY A T168 G188 R196 D199 G220 G222 T156 G176 R184 D187 G208 G210
BS02 GLY A S88 A89 M109 H114 C115 S89 A90 M110 H115 C116
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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Cellular Component
External links
PDB RCSB:4o0f, PDBe:4o0f, PDBj:4o0f
PDBsum4o0f
PubMed24768817
UniProtQ7L266|ASGL1_HUMAN Isoaspartyl peptidase/L-asparaginase (Gene Name=ASRGL1)

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