Structure of PDB 4o0f Chain B Binding Site BS01

Receptor Information
>4o0f Chain B (length=293) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HMNPIVVVHGGGAGPISKDRKERVHQGMVRAATVGYGILREGGSAVDAVE
GAVVALEDDPEFNAGCGSVLNTNGEVEMDASIMDGKDLSAGAVSAVQCIA
NPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVTERNKKRLE
KEKGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDI
GAVSTAGHGESILKVNLARLTLFHIEQGKTVEEAADLSLGYMKSRVKGLG
GLIVVSKTGDWVAKWTSTSMPWAAAKDGKLHFGIDPTTITDLP
Ligand information
Ligand IDGLY
InChIInChI=1S/C2H5NO2/c3-1-2(4)5/h1,3H2,(H,4,5)
InChIKeyDHMQDGOQFOQNFH-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(C(=O)O)N
CACTVS 3.341NCC(O)=O
ACDLabs 10.04O=C(O)CN
FormulaC2 H5 N O2
NameGLYCINE
ChEMBLCHEMBL773
DrugBankDB00145
ZINCZINC000004658552
PDB chain4o0f Chain B Residue 403 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4o0f Elucidation of the Specific Function of the Conserved Threonine Triad Responsible for Human l-Asparaginase Autocleavage and Substrate Hydrolysis.
Resolution1.92 Å
Binding residue
(original residue number in PDB)		A89 M109 H114 C115
Binding residue
(residue number reindexed from 1)		A90 M110 H115 C116
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) N62 T168 T186 R196 A219 G220
Catalytic site (residue number reindexed from 1) N63 T155 T173 R183 A206 G207
Enzyme Commision number 3.4.19.5: beta-aspartyl-peptidase.
3.5.1.1: asparaginase.
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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Molecular Function
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Biological Process
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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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