 |
PDBsum entry 1v0n
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
PDB id:
|
 |
|
 |
| Name: |
 |
Hydrolase
|
 |
|
Title:
|
 |
Xylanase xyn10a from streptomyces lividans in complex with xylobio- isofagomine at ph 7.5
|
|
Structure:
|
 |
Endo-1,4-beta-xylanase a. Chain: a. Fragment: catalytic module, residues 42-354. Synonym: xylanase a, 1,4-beta-d-xylan xylanohydrolase a. Engineered: yes
|
|
Source:
|
 |
Streptomyces lividans. Organism_taxid: 1916. Expressed in: streptomyces lividans. Expression_system_taxid: 1916.
|
|
Resolution:
|
 |
|
1.10Å
|
R-factor:
|
0.104
|
R-free:
|
0.124
|
|
|
Authors:
|
 |
T.M.Gloster,S.J.Williams,S.Roberts,C.A.Tarling,J.Wicki,S.G.Withers, G.J.Davies
|
|
Key ref:
|
 |
T.M.Gloster
et al.
(2004).
Atomic resolution analyses of the binding of xylobiose-derived deoxynojirimycin and isofagomine to xylanase Xyn10A.
Chem Commun (camb),
16,
1794-1795.
PubMed id:
|
 |
|
Date:
|
 |
|
31-Mar-04
|
Release date:
|
16-Aug-04
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
Headers
|
 |
|
|
References
|
|
|
|
|
|
|
P26514
(XYNA_STRLI) -
Endo-1,4-beta-xylanase A from Streptomyces lividans
|
|
|
|
Seq: Struc:
|
 |
 |
 |
477 a.a.
302 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
Key: |
 |
PfamA domain |
 |
 |
 |
Secondary structure |
 |
 |
CATH domain |
 |
|
|
|
|
 |
|
|
 |
 |
 |
 |
Enzyme class:
|
 |
E.C.3.2.1.8
- endo-1,4-beta-xylanase.
|
|
 |
 |
 |
 |
 |
Reaction:
|
 |
Endohydrolysis of 1,4-beta-D-xylosidic linkages in xylans.
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
| |
|
|
Chem Commun (camb)
16:1794-1795
(2004)
|
|
PubMed id:
|
|
|
|
|
| |
|
Atomic resolution analyses of the binding of xylobiose-derived deoxynojirimycin and isofagomine to xylanase Xyn10A.
|
|
T.M.Gloster,
S.J.Williams,
S.Roberts,
C.A.Tarling,
J.Wicki,
S.G.Withers,
G.J.Davies.
|
|
|
|
| |
ABSTRACT
|
|
|
| |
|
The atomic resolution structures of xylobiose-derived isofagomine and
xylobiose-derived deoxynojirimycin in complex with the xylanase Xyn10A from
Streptomyces lividans reveal undistorted (4)C(1) chair conformed sugars and, in
the case of the deoxynojirimycin analogue, suggest unusual pK(a) changes of the
enzyme's catalytic machinery upon binding.
|
|
|
|
|
|
|
 |
 |
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
 |
| |
PubMed id
|
 |
Reference
|
 |
|
|
|
 |
M.Aguilar-Moncayo,
T.M.Gloster,
J.P.Turkenburg,
M.I.García-Moreno,
C.Ortiz Mellet,
G.J.Davies,
and
J.M.García Fernández
(2009).
Glycosidase inhibition by ring-modified castanospermine analogues: tackling enzyme selectivity by inhibitor tailoring.
|
| |
Org Biomol Chem,
7,
2738-2747.
|
 |
|
PDB codes:
|
 |
|
|
|
|
|
 |
A.D.Hill,
and
P.J.Reilly
(2008).
A Gibbs free energy correlation for automated docking of carbohydrates.
|
| |
J Comput Chem,
29,
1131-1141.
|
 |
|
 |
 |
|
The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
|
');
}
}
 |