Structure of PDB 2o53 Chain B

Receptor sequence
>2o53B (length=302) Species: 9606 (Homo sapiens) [Search protein sequence]
EHIQKVAIFGGTHGNELTGVFLVKHWLENGAEIQRTGLEVKPFITNPRAV
KKCTRYIDCDLNRIFDLENLGKKMSEDLPYEVRRAQEINHLFGPKDSEDS
YDIIFDLHNTTSNMGCTLILEDSRNNFLIQMFHYIKTSLAPLPCYVYLIE
HPSLKYATTRSIAKYPVGIEVGPQPQGVLRADILDQMRKMIKHALDFIHH
FNEGKEFPPCAIEVYKIIEKVDYPRDENGEIAAIIHPNLQDQDWKPLHPG
DPMFLTLDGKTIPLGGDCTVYPVFVNEAAYYEKKEAFAKTTKLTLNAKSI
RC
3D structure
PDB2o53 Examination of the Mechanism of Human Brain Aspartoacylase through the Binding of an Intermediate Analogue.
ChainB
Resolution2.7 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.5.1.15: aspartoacylase.
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 ZN B H21 E24 H116 H13 E16 H108
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0016787 hydrolase activity
GO:0016788 hydrolase activity, acting on ester bonds
GO:0016811 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
GO:0019807 aspartoacylase activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0006083 acetate metabolic process
GO:0006531 aspartate metabolic process
GO:0022010 central nervous system myelination
GO:0048714 positive regulation of oligodendrocyte differentiation
Cellular Component
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:2o53, PDBe:2o53, PDBj:2o53
PDBsum2o53
PubMed18293939
UniProtP45381|ACY2_HUMAN Aspartoacylase (Gene Name=ASPA)

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