Structure of PDB 3nfz Chain A

Receptor sequence
>3nfzA (length=305) Species: 10090 (Mus musculus) [Search protein sequence]
SREPLLRVAVTGGTHGNEMCGVYLARYWLQNPGELQRPSFSAMPVLANPA
ATAACCRYLDRDLNRSCTLTFLGSTATPDDPYEVKRARELNQLLGPKGTG
QAFDFTLDLHNTTANTGVCLISESNISFNLHLCHYLQRQNPGMPCRLFLY
EPAGTETFSVESISKNGICLAMGPQPQGVLRADLFSRMRALVASILDFIE
LFNQGMDLPAFEMDIYRNLGSVDFPRTADGDLAGTVHPQLQDHDFEPLRP
GEPIFKLFSGEDVLYEGDSIVYPVFINEAAYYEKHVAFLKSEKIRVTVPA
LLRLT
3D structure
PDB3nfz Structures of aminoacylase 3 in complex with acetylated substrates.
ChainA
Resolution2.147 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.5.1.114: N-acyl-aromatic-L-amino acid amidohydrolase.
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 H15 E18 H110
BS02 3NF A H21 R63 N70 R71 I127 E129 E284 Y287 H15 R57 N64 R65 I121 E123 E278 Y281
Gene Ontology
Molecular Function
GO:0004046 aminoacylase activity
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:0042802 identical protein binding
GO:0046872 metal ion binding
Cellular Component
GO:0005737 cytoplasm
GO:0005886 plasma membrane
GO:0016020 membrane
GO:0016324 apical plasma membrane

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Molecular Function
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Cellular Component
External links
PDB RCSB:3nfz, PDBe:3nfz, PDBj:3nfz
PDBsum3nfz
PubMed20921362
UniProtQ91XE4|ACY3_MOUSE N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming) (Gene Name=Acy3)

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