Structure of PDB 4nfr Chain B

Receptor sequence
>4nfrB (length=301) Species: 9606 (Homo sapiens) [Search protein sequence]
HIQKVAIFGGTHGNELTGVFLVKHWLENGAEIQRTGLEVKPFITNPRAVK
KCTRYIDCDLNRIFDLENLGKKMSEDLPYEVRRAQEINHLFGPKDSEDSY
DIIFDLHNTTSNMGCTLILEDSRNNFLIQMFHYIKTSLAPLPCYVYLIEH
PSLKYATTRSIAKYPVGIEVGPQPQGVLRADILDQMRKMIKHALDFIHHF
NEGKEFPPCAIEVYKIIEKVDYPRDENGEIAAIIHPNLQDQDWKPLHPGD
PMFLTLDGKTIPLGGDCTVYPVFVNAAAYYEKKEAFAKTTKLTLNAKSIR
C
3D structure
PDB4nfr Aspartoacylase catalytic deficiency as the cause of canavan disease: a structural perspective.
ChainB
Resolution3.0 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 AS9 B H21 R63 N70 H116 Y164 R168 E178 H12 R54 N61 H107 Y155 R159 E169
BS02 ZN B H21 E24 H116 H12 E15 H107
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4nfr, PDBe:4nfr, PDBj:4nfr
PDBsum4nfr
PubMed25003821
UniProtP45381|ACY2_HUMAN Aspartoacylase (Gene Name=ASPA)

[Back to BioLiP]