Structure of PDB 4osx Chain A

Receptor sequence
>4osxA (length=300) Species: 9606 (Homo sapiens) [Search protein sequence]
HMNPIVVVHGGGAGPISKDRKERVHQGMVRAATVGYGILREGGSAVDAVE
GAVVALEDDPEFNAGCGSVLNTNGEVEMDASIMDGKDLSAGAVSAVQCIA
NPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVTERNKKRLE
KEKHQKNLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGY
ADNDIGAVSTTGHGESILKVNLARLTLFHIEQGKTVEEAADLSLGYMKSR
VKGLGGLIVVSKTGDWVAKWTSTSMPWAAAKDGKLHFGIDPDDTTITDLP
3D structure
PDB4osx Free Glycine Accelerates the Autoproteolytic Activation of Human Asparaginase.
ChainA
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 T168 T186 R196 T219 G220
Catalytic site (residue number reindexed from 1) N63 T160 T178 R188 T211 G212
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 T186 R196 D199 T178 R188 D191
BS02 GLY A G10 L166 G167 T168 T219 G220 G11 L158 G159 T160 T211 G212
BS03 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:4osx, PDBe:4osx, PDBj:4osx
PDBsum4osx
PubMed23601642
UniProtQ7L266|ASGL1_HUMAN Isoaspartyl peptidase/L-asparaginase (Gene Name=ASRGL1)

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