Structure of PDB 4o0d Chain B

Receptor sequence
>4o0dB (length=298) Species: 9606 (Homo sapiens) [Search protein sequence]
HMNPIVVVHGGGAGPISKDRKERVHQGMVRAATVGYGILREGGSAVDAVE
GAVVALEDDPEFNAGCGSVLNTNGEVEMDASIMDGKDLSAGAVSAVQCIA
NPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVTERNKKRLE
KEKHELGSVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYAD
NDIGAVSTTGHGESILKVNLARLTLFHIEQGKTVEEAADLSLGYMKSRVK
GLGGLIVVSKTGDWVAKWTSTSMPWAAAKDGKLHFGIDPDDTTITDLP
3D structure
PDB4o0d Elucidation of the Specific Function of the Conserved Threonine Triad Responsible for Human l-Asparaginase Autocleavage and Substrate Hydrolysis.
ChainB
Resolution1.95 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 S168 T186 R196 T219 G220
Catalytic site (residue number reindexed from 1) N63 S158 T176 R186 T209 G210
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 B S88 A89 M109 T112 H114 C115 S89 A90 M110 T113 H115 C116
BS02 GLY B S168 R196 D199 G222 S158 R186 D189 G212
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:4o0d, PDBe:4o0d, PDBj:4o0d
PDBsum4o0d
PubMed24768817
UniProtQ7L266|ASGL1_HUMAN Isoaspartyl peptidase/L-asparaginase (Gene Name=ASRGL1)

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