PDBsum entry 1pp4

Go to PDB code: 
protein ligands Protein-protein interface(s) links
Hydrolase PDB id
Protein chains
233 a.a. *
NAG ×4
Waters ×59
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: The crystal structure of rhamnogalacturonan acetylesterase i group p3121
Structure: Rhamnogalacturonan acetylesterase. Chain: a, b. Synonym: rgae. Engineered: yes
Source: Aspergillus aculeatus. Organism_taxid: 5053. Gene: rha1. Expressed in: aspergillus oryzae. Expression_system_taxid: 5062.
2.50Å     R-factor:   0.182     R-free:   0.222
Authors: A.Molgaard,S.Larsen
Key ref:
A.Mølgaard and S.Larsen (2004). Crystal packing in two pH-dependent crystal forms of rhamnogalacturonan acetylesterase. Acta Crystallogr D Biol Crystallogr, 60, 472-478. PubMed id: 14993671 DOI: 10.1107/S0907444903029767
16-Jun-03     Release date:   02-Mar-04    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
Q00017  (RHA1_ASPAC) -  Rhamnogalacturonan acetylesterase
250 a.a.
233 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Rhamnogalacturonan acetylesterase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     lipid metabolic process   1 term 
  Biochemical function     hydrolase activity     2 terms  


DOI no: 10.1107/S0907444903029767 Acta Crystallogr D Biol Crystallogr 60:472-478 (2004)
PubMed id: 14993671  
Crystal packing in two pH-dependent crystal forms of rhamnogalacturonan acetylesterase.
A.Mølgaard, S.Larsen.
The glycoprotein rhamnogalacturonan acetylesterase from Aspergillus aculeatus has been crystallized in two crystal forms, an orthorhombic and a trigonal crystal form. In the orthorhombic crystal form, the covalently bound carbohydrate at one of the two N-glycosylation sites is involved in crystal contacts. The orthorhombic crystal form was obtained at pH 5.0 and the trigonal crystal form at pH 4.5. In one case, the two crystal forms were found in the same drop at pH 4.7. The differences in crystal packing in the two crystal forms can be explained by the pH-dependent variation in the protonation state of the glutamic acid residues on the protein surface.
  Selected figure(s)  
Figure 3.
Figure 3 An overlay of the orthorhombic (yellow) and the trigonal (purple) crystal form at the trigonal AA and BB crystal contacts. The figure was prepared using the program MOLSCRIPT (Kraulis, 1991[Kraulis, P. (1991). J. Appl. Cryst. 24, 946-950.]).
  The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2004, 60, 472-478) copyright 2004.  
  Figure was selected by an automated process.