Structure of PDB 2q4z Chain B

Receptor sequence
>2q4zB (length=307) Species: 10116 (Rattus norvegicus) [Search protein sequence]
CVAEEPIKKIAIFGGTHGNELTGVFLVTHWLKNGAEVHRAGLEVKPFITN
PRAVEKCTRYIDCDLNRVFDLENLSKEMSEDLPYEVRRAQEINHLFGPKN
SDDAYDVVFDLHNTTSNMGCTLILGDSGNDFLIQMFHYIKTCMAPLPCSV
YLIEHPSLKYATTRSIAKYPVGIEVGPQPHGVLRADILDQMRRMLKHALD
FIQRFNEGKEFPPCAIDVYKIMEKVDYPRNESGDVAAVIHPNLQDQDWKP
LHPGDPVFVSLDGKVIPLGGDCTVYPVFVNEAAYYEKKEAFAKTTKLTLN
AKSIRST
3D structure
PDB2q4z Ensemble refinement of protein crystal structures: validation and application.
ChainB
Resolution1.8 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 H20 E23 H17 E20
Gene Ontology
Molecular Function
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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Cellular Component
External links
PDB RCSB:2q4z, PDBe:2q4z, PDBj:2q4z
PDBsum2q4z
PubMed17850744
UniProtQ9R1T5|ACY2_RAT Aspartoacylase (Gene Name=Aspa)

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