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PDBsum entry 3nh4

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protein ligands metals links
Hydrolase PDB id
3nh4

 

 

 

 

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Contents
Protein chain
303 a.a. *
Ligands
ACT
FMT
Metals
_ZN
_CS ×2
_CL ×2
Waters ×95
* Residue conservation analysis
PDB id:
3nh4
Name: Hydrolase
Title: Crystal structure of murine aminoacylase 3
Structure: Aspartoacylase-2. Chain: a. Synonym: aminoacylase-3, acy-3, aminoacylase iii, acylase iii, hepatitis c virus core-binding protein 1, hcbp1. Engineered: yes
Source: Mus musculus. Mouse. Organism_taxid: 10090. Gene: acy-3, acy3, aspa2. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.00Å     R-factor:   0.186     R-free:   0.207
Authors: J.M.Hsieh,K.Tsirulnikov,M.R.Sawaya,N.Magilnick,N.Abuladze,I.Kurtz, J.Abramson,A.Pushkin
Key ref: J.M.Hsieh et al. (2010). Structures of aminoacylase 3 in complex with acetylated substrates. Proc Natl Acad Sci U S A, 107, 17962-17967. PubMed id: 20921362
Date:
14-Jun-10     Release date:   20-Oct-10    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q91XE4  (ACY3_MOUSE) -  N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming) from Mus musculus
Seq:
Struc:
318 a.a.
303 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.5.1.114  - N-acyl-aromatic-L-amino acid amidohydrolase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction:
1. an N-acyl-aromatic L-alpha-amino acid + H2O = an aromatic L-alpha- amino acid + a carboxylate
2. an N-acetyl-L-cysteine-S-conjugate + H2O = an S-substituted L-cysteine + acetate
N-acyl-aromatic L-alpha-amino acid
+ H2O
= aromatic L-alpha- amino acid
Bound ligand (Het Group name = ACT)
matches with 60.00% similarity
+ carboxylate
N-acetyl-L-cysteine-S-conjugate
+ H2O
=
S-substituted L-cysteine
Bound ligand (Het Group name = ACT)
corresponds exactly
+ acetate
      Cofactor: Zn(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Proc Natl Acad Sci U S A 107:17962-17967 (2010)
PubMed id: 20921362  
 
 
Structures of aminoacylase 3 in complex with acetylated substrates.
J.M.Hsieh, K.Tsirulnikov, M.R.Sawaya, N.Magilnick, N.Abuladze, I.Kurtz, J.Abramson, A.Pushkin.
 
  ABSTRACT  
 
No abstract given.

 

 

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