Structure of PDB 2o4h Chain A

Receptor sequence
>2o4hA (length=301) Species: 9606 (Homo sapiens) [Search protein sequence]
HIQKVAIFGGTHGNELTGVFLVKHWLENGAEIQRTGLEVKPFITNPRAVK
KCTRYIDCDLNRIFDLENLGKKMSEDLPYEVRRAQEINHLFGPKDSEDSY
DIIFDLHNTTSNMGCTLILEDSRNNFLIQMFHYIKTSLAPLPCYVYLIEH
PSLKYATTRSIAKYPVGIEVGPQPQGVLRADILDQMRKMIKHALDFIHHF
NEGKEFPPCAIEVYKIIEKVDYPRDENGEIAAIIHPNLQDQDWKPLHPGD
PMFLTLDGKTIPLGGDCTVYPVFVNEAAYYEKKEAFAKTTKLTLNAKSIR
C
3D structure
PDB2o4h Examination of the Mechanism of Human Brain Aspartoacylase through the Binding of an Intermediate Analogue.
ChainA
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 A H21 E24 H116 H12 E15 H107
BS02 AS9 A H21 E24 R63 N70 R71 H116 N117 I127 Y164 R168 E178 E285 Y288 H12 E15 R54 N61 R62 H107 N108 I118 Y155 R159 E169 E276 Y279 PDBbind-CN: -logKd/Ki=6.52,Ki=300nM
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:2o4h, PDBe:2o4h, PDBj:2o4h
PDBsum2o4h
PubMed18293939
UniProtP45381|ACY2_HUMAN Aspartoacylase (Gene Name=ASPA)

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