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PDBsum entry 3ju4

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protein ligands metals links
Hydrolase PDB id
3ju4
Jmol
Contents
Protein chain
670 a.a. *
Ligands
SLB
Metals
_NA
_CL ×5
Waters ×1616
* Residue conservation analysis
PDB id:
3ju4
Name: Hydrolase
Title: Crystal structure analysis of endosialidasenf at 0.98 a reso
Structure: Endo-n-acetylneuraminidase. Chain: a. Fragment: unp residues 246-910. Synonym: endonf, endo-n, endosialidase, g102. Engineered: yes
Source: Enterobacteria phage k1f. Bacteriophage k1f. Organism_taxid: 344021. Strain: k1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
0.98Å     R-factor:   0.116     R-free:   0.133
Authors: E.C.Schulz,P.Neuman,R.Gerardy-Schahn,G.M.Sheldrick,R.Ficner
Key ref: E.C.Schulz et al. (2010). Structure analysis of endosialidase NF at 0.98 A resolution. Acta Crystallogr D Biol Crystallogr, 66, 176-180. PubMed id: 20124697
Date:
14-Sep-09     Release date:   02-Feb-10    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q04830  (ENAN_BPK1F) -  Endo-N-acetylneuraminidase
Seq:
Struc:
 
Seq:
Struc:
920 a.a.
670 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.129  - Endo-alpha-sialidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Endohydrolysis of (2->8)-alpha-sialosyl linkages in oligo- or poly(sialic) acids.

 

 
Acta Crystallogr D Biol Crystallogr 66:176-180 (2010)
PubMed id: 20124697  
 
 
Structure analysis of endosialidase NF at 0.98 A resolution.
E.C.Schulz, P.Neumann, R.Gerardy-Schahn, G.M.Sheldrick, R.Ficner.
 
  ABSTRACT  
 
Endosialidase NF (endoNF) is a bacteriophage-derived endosialidase that specifically degrades alpha-2,8-linked polysialic acid. The structure of a new crystal form of endoNF in complex with sialic acid has been refined at 0.98 A resolution. The 210 kDa homotrimeric multi-domain enzyme displays outstanding stability and resistance to SDS. Even at atomic resolution, only a minor fraction of side chains possess alternative conformations. However, multiple conformations of an active-site residue imply that it has an important catalytic function in the cleavage mechanism of polysialic acid.