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PDBsum entry 3nvd
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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
3nvd

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
617 a.a. *
Ligands
OAN ×2
PG4
ACT ×4
Metals
_NA ×2
Waters ×1527
* Residue conservation analysis
PDB id:
3nvd
Name: Hydrolase
Title: Structure of ybbd in complex with pugnac
Structure: Uncharacterized lipoprotein ybbd. Chain: a, b. Synonym: orf1. Engineered: yes
Source: Bacillus subtilis. Organism_taxid: 1423. Strain: wt168. Gene: ybbd. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.84Å     R-factor:   0.191     R-free:   0.246
Authors: K.Diederichs
Key ref: S.Litzinger et al. (2010). Structural and kinetic analysis of Bacillus subtilis N-acetylglucosaminidase reveals a unique Asp-His dyad mechanism. J Biol Chem, 285, 35675-35684. PubMed id: 20826810
Date:
08-Jul-10     Release date:   04-Aug-10    
Supersedes: 3cqm
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P40406  (NAGZ_BACSU) -  Beta-hexosaminidase from Bacillus subtilis (strain 168)
Seq:
Struc: 		 
Seq:
Struc: 		642 a.a.
617 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.52  - beta-N-acetylhexosaminidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.

 

 
J Biol Chem 285:35675-35684 (2010)
PubMed id: 20826810  
 
 
Structural and kinetic analysis of Bacillus subtilis N-acetylglucosaminidase reveals a unique Asp-His dyad mechanism.
S.Litzinger, S.Fischer, P.Polzer, K.Diederichs, W.Welte, C.Mayer.
 
  ABSTRACT  
 
No abstract given.

 

 

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