spacer
spacer

PDBsum entry 3ug3

Go to PDB code: 
protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
3ug3

 

 

 

 

Loading ...

 
JSmol PyMol  
Contents
Protein chains
(+ 0 more) 482 a.a.
Ligands
TRS ×6
EDO ×51
Metals
_NA
Waters ×2424
PDB id:
3ug3
Name: Hydrolase
Title: Crystal structure of alpha-l-arabinofuranosidase from thermotoga maritima ligand free form
Structure: Alpha-l-arabinofuranosidase. Chain: a, b, c, d, e, f. Engineered: yes. Mutation: yes
Source: Thermotoga maritima. Organism_taxid: 2336. Strain: msb8. Gene: tm_0281. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.80Å     R-factor:   0.176     R-free:   0.197
Authors: D.-H.Im,K.Miyazaki,T.Wakagi,S.Fushinobu
Key ref: D.H.Im et al. (2012). Crystal structures of glycoside hydrolase family 51 α-L-arabinofuranosidase from Thermotoga maritima. Biosci Biotechnol Biochem, 76, 423-428. PubMed id: 22313787
Date:
02-Nov-11     Release date:   07-Mar-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9WYB7  (Q9WYB7_THEMA) -  Alpha-L-arabinofuranosidase from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
Seq:
Struc:
484 a.a.
482 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.55  - non-reducing end alpha-L-arabinofuranosidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.

 

 
Biosci Biotechnol Biochem 76:423-428 (2012)
PubMed id: 22313787  
 
 
Crystal structures of glycoside hydrolase family 51 α-L-arabinofuranosidase from Thermotoga maritima.
D.H.Im, K.Kimura, F.Hayasaka, T.Tanaka, M.Noguchi, A.Kobayashi, S.Shoda, K.Miyazaki, T.Wakagi, S.Fushinobu.
 
  ABSTRACT  
 
No abstract given.

 

 

spacer

spacer