Structure of PDB 4mri Chain A

Receptor sequence

>4mriA (length=302) Species: 9606 (Homo sapiens)

HIQKVAIFGGTHGNELTGVFLVKHWLENGAEIQRTGLEVKPFITNPRAVK
KCTRYIDCDLNRIFDLENLGKKMSEDLPYEVRRAQEINHLFGPKDSEDSY
DIIFDLHNTTSNMGCTLILEDSRNNFLIQMFHYIKTSLAPLPCYVYLIEH
PSLKYATTRSIAKYPVGIEVGPQPQGVLRADILDQMRKMIKHALDFIHHF
NEGKEFPPCAIEVYKIIEKVDYPRDENGEIAAIIHPNLQDQDWKPLHPGD
PMFLTLDGKTIPLGGDCTVYPVFVNEAAYYEKKEASAKTTKLTLNAKSIR
CC

3D structure

• PDB: 4mri Aspartoacylase catalytic deficiency as the cause of canavan disease: a structural perspective.
• Chain: A
• Resolution: 2.8 Å

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 Y164 R168 E178 E285 Y288	H12 E15 R54 N61 R62 H107 N108 Y155 R159 E169 E276 Y279

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

External links

• PDB: RCSB:4mri, PDBe:4mri, PDBj:4mri
• PDBsum: 4mri
• PubMed: 25003821
• UniProt: P45381|ACY2_HUMAN Aspartoacylase (Gene Name=ASPA)