|
Atomistry » Chlorine » PDB 5bvf-5c2b » 5c1e | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 5bvf-5c2b » 5c1e » |
Chlorine in PDB 5c1e: Crystal Structure of the Pectin Methylesterase From Aspergillus Niger in Penultimately Deglycosylated Form (N-Acetylglucosamine Stub at ASN84)Enzymatic activity of Crystal Structure of the Pectin Methylesterase From Aspergillus Niger in Penultimately Deglycosylated Form (N-Acetylglucosamine Stub at ASN84)
All present enzymatic activity of Crystal Structure of the Pectin Methylesterase From Aspergillus Niger in Penultimately Deglycosylated Form (N-Acetylglucosamine Stub at ASN84):
3.1.1.11; Protein crystallography data
The structure of Crystal Structure of the Pectin Methylesterase From Aspergillus Niger in Penultimately Deglycosylated Form (N-Acetylglucosamine Stub at ASN84), PDB code: 5c1e
was solved by
G.B.Jameson,
M.A.K.Williams,
T.S.Loo,
L.M.Kent,
L.D.Melton,
D.Mercadante,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of the Pectin Methylesterase From Aspergillus Niger in Penultimately Deglycosylated Form (N-Acetylglucosamine Stub at ASN84)
(pdb code 5c1e). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of the Pectin Methylesterase From Aspergillus Niger in Penultimately Deglycosylated Form (N-Acetylglucosamine Stub at ASN84), PDB code: 5c1e: Chlorine binding site 1 out of 1 in 5c1eGo back to Chlorine Binding Sites List in 5c1e
Chlorine binding site 1 out
of 1 in the Crystal Structure of the Pectin Methylesterase From Aspergillus Niger in Penultimately Deglycosylated Form (N-Acetylglucosamine Stub at ASN84)
Mono view Stereo pair view
Reference:
L.M.Kent,
T.S.Loo,
L.D.Melton,
D.Mercadante,
M.A.Williams,
G.B.Jameson.
Structure and Properties of A Non-Processive, Salt-Requiring, and Acidophilic Pectin Methylesterase From Aspergillus Niger Provide Insights Into the Key Determinants of Processivity Control. J.Biol.Chem. V. 291 1289 2016.
Page generated: Fri Jul 26 05:50:45 2024
ISSN: ESSN 1083-351X PubMed: 26567911 DOI: 10.1074/JBC.M115.673152 |
Last articlesZn in 9JPJZn in 9JP7 Zn in 9JPK Zn in 9JPL Zn in 9GN6 Zn in 9GN7 Zn in 9GKU Zn in 9GKW Zn in 9GKX Zn in 9GL0 |
© Copyright 2008-2020 by atomistry.com | ||
Home | Site Map | Copyright | Contact us | Privacy |