Structure of PDB 4mri Chain B

Receptor sequence
>4mriB (length=303) Species: 9606 (Homo sapiens) [Search protein sequence]
EHIQKVAIFGGTHGNELTGVFLVKHWLENGAEIQRTGLEVKPFITNPRAV
KKCTRYIDCDLNRIFDLENLGKKMSEDLPYEVRRAQEINHLFGPKDSEDS
YDIIFDLHNTTSNMGCTLILEDSRNNFLIQMFHYIKTSLAPLPCYVYLIE
HPSLKYATTRSIAKYPVGIEVGPQPQGVLRADILDQMRKMIKHALDFIHH
FNEGKEFPPCAIEVYKIIEKVDYPRDENGEIAAIIHPNLQDQDWKPLHPG
DPMFLTLDGKTIPLGGDCTVYPVFVNEAAYYEKKEASAKTTKLTLNAKSI
RCC
3D structure
PDB4mri Aspartoacylase catalytic deficiency as the cause of canavan disease: a structural perspective.
ChainB
Resolution2.8 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
BS02 AS9 B H21 E24 R63 N70 R71 H116 N117 I127 Y164 R168 E178 E285 Y288 H13 E16 R55 N62 R63 H108 N109 I119 Y156 R160 E170 E277 Y280
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:4mri, PDBe:4mri, PDBj:4mri
PDBsum4mri
PubMed25003821
UniProtP45381|ACY2_HUMAN Aspartoacylase (Gene Name=ASPA)

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