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Atomistry » Sodium » PDB 4hfd-4i05 » 4hmd | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Sodium » PDB 4hfd-4i05 » 4hmd » |
Sodium in PDB 4hmd: Crystal Structure of Cold-Adapted Chitinase From Moritella Marina with A Reaction Intermediate - Oxazolinium Ion (Ngo)Enzymatic activity of Crystal Structure of Cold-Adapted Chitinase From Moritella Marina with A Reaction Intermediate - Oxazolinium Ion (Ngo)
All present enzymatic activity of Crystal Structure of Cold-Adapted Chitinase From Moritella Marina with A Reaction Intermediate - Oxazolinium Ion (Ngo):
3.2.1.14; Protein crystallography data
The structure of Crystal Structure of Cold-Adapted Chitinase From Moritella Marina with A Reaction Intermediate - Oxazolinium Ion (Ngo), PDB code: 4hmd
was solved by
P.H.Malecki,
C.E.Vorgias,
J.E.Raczynska,
W.Rypniewski,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Sodium Binding Sites:
The binding sites of Sodium atom in the Crystal Structure of Cold-Adapted Chitinase From Moritella Marina with A Reaction Intermediate - Oxazolinium Ion (Ngo)
(pdb code 4hmd). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of Cold-Adapted Chitinase From Moritella Marina with A Reaction Intermediate - Oxazolinium Ion (Ngo), PDB code: 4hmd: Sodium binding site 1 out of 1 in 4hmdGo back to Sodium Binding Sites List in 4hmd
Sodium binding site 1 out
of 1 in the Crystal Structure of Cold-Adapted Chitinase From Moritella Marina with A Reaction Intermediate - Oxazolinium Ion (Ngo)
Mono view Stereo pair view
Reference:
P.H.Malecki,
J.E.Raczynska,
C.E.Vorgias,
W.Rypniewski.
Structure of A Complete Four-Domain Chitinase From Moritella Marina, A Marine Psychrophilic Bacterium Acta Crystallogr.,Sect.D V. 69 821 2013.
Page generated: Tue Dec 15 06:43:31 2020
ISSN: ISSN 0907-4449 PubMed: 23633591 DOI: 10.1107/S0907444913002011 |
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