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Atomistry » Zinc » PDB 1sdx-1sx1 » 1smp » |
Zinc in PDB 1smp: Crystal Structure of A Complex Between Serratia Marcescens Metallo-Protease and An Inhibitor From Erwinia ChrysanthemiEnzymatic activity of Crystal Structure of A Complex Between Serratia Marcescens Metallo-Protease and An Inhibitor From Erwinia Chrysanthemi
All present enzymatic activity of Crystal Structure of A Complex Between Serratia Marcescens Metallo-Protease and An Inhibitor From Erwinia Chrysanthemi:
3.4.24.40; Protein crystallography data
The structure of Crystal Structure of A Complex Between Serratia Marcescens Metallo-Protease and An Inhibitor From Erwinia Chrysanthemi, PDB code: 1smp
was solved by
U.Baumann,
M.Bauer,
S.Letoffe,
P.Delepelaire,
C.Wandersman,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1smp:
The structure of Crystal Structure of A Complex Between Serratia Marcescens Metallo-Protease and An Inhibitor From Erwinia Chrysanthemi also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of A Complex Between Serratia Marcescens Metallo-Protease and An Inhibitor From Erwinia Chrysanthemi
(pdb code 1smp). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of A Complex Between Serratia Marcescens Metallo-Protease and An Inhibitor From Erwinia Chrysanthemi, PDB code: 1smp: Zinc binding site 1 out of 1 in 1smpGo back to![]() ![]()
Zinc binding site 1 out
of 1 in the Crystal Structure of A Complex Between Serratia Marcescens Metallo-Protease and An Inhibitor From Erwinia Chrysanthemi
![]() Mono view ![]() Stereo pair view
Reference:
U.Baumann,
M.Bauer,
S.Letoffe,
P.Delepelaire,
C.Wandersman.
Crystal Structure of A Complex Between Serratia Marcescens Metallo-Protease and An Inhibitor From Erwinia Chrysanthemi. J.Mol.Biol. V. 248 653 1995.
Page generated: Wed Dec 16 03:03:40 2020
ISSN: ISSN 0022-2836 PubMed: 7752231 DOI: 10.1006/JMBI.1995.0249 |
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