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PDBsum entry 4as2

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
4as2

 

 

 

 

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Contents
Protein chains
327 a.a.
Ligands
BTB ×8
Metals
IOD ×13
_MG ×4
_CL ×4
Waters ×814
PDB id:
4as2
Name: Hydrolase
Title: Pseudomonas aeruginosa phosphorylcholine phosphatase. Monoclinic form
Structure: Phosphorylcholine phosphatase. Chain: a, b, c, d. Fragment: residues 23-349. Engineered: yes
Source: Pseudomonas aeruginosa. Organism_taxid: 287. Expressed in: escherichia coli. Expression_system_taxid: 511693. Expression_system_variant: codonplus.
Resolution:
2.12Å     R-factor:   0.157     R-free:   0.210
Authors: L.Infantes,L.H.Otero,A.Albert
Key ref: L.Infantes et al. (2012). The structural domains of Pseudomonas aeruginosa phosphorylcholine phosphatase cooperate in substrate hydrolysis: 3D structure and enzymatic mechanism. J Mol Biol, 423, 503-514. PubMed id: 22922065
Date:
27-Apr-12     Release date:   22-Aug-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Q9HTR2  (PCHP_PSEAE) -  Phosphorylcholine phosphatase from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Seq:
Struc:
349 a.a.
327 a.a.
Key:    Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.1.3.75  - phosphoethanolamine/phosphocholine phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction:
1. phosphoethanolamine + H2O = ethanolamine + phosphate
2. phosphocholine + H2O = choline + phosphate
phosphoethanolamine
+ H2O
= ethanolamine
+ phosphate
phosphocholine
+ H2O
=
choline
Bound ligand (Het Group name = BTB)
matches with 40.00% similarity
+ phosphate
      Cofactor: Mg(2+) or cobalt cation or Mn(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
J Mol Biol 423:503-514 (2012)
PubMed id: 22922065  
 
 
The structural domains of Pseudomonas aeruginosa phosphorylcholine phosphatase cooperate in substrate hydrolysis: 3D structure and enzymatic mechanism.
L.Infantes, L.H.Otero, P.R.Beassoni, C.Boetsch, A.T.Lisa, C.E.Domenech, A.Albert.
 
  ABSTRACT  
 
No abstract given.

 

 

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