|
Atomistry » Calcium » PDB 1fak-1fn6 » 1fm1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 1fak-1fn6 » 1fm1 » |
Calcium in PDB 1fm1: Solution Structure of the Catalytic Fragment of Human Collagenase-3 (Mmp-13) Complexed with A Hydroxamic Acid InhibitorOther elements in 1fm1:
The structure of Solution Structure of the Catalytic Fragment of Human Collagenase-3 (Mmp-13) Complexed with A Hydroxamic Acid Inhibitor also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Solution Structure of the Catalytic Fragment of Human Collagenase-3 (Mmp-13) Complexed with A Hydroxamic Acid Inhibitor
(pdb code 1fm1). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Solution Structure of the Catalytic Fragment of Human Collagenase-3 (Mmp-13) Complexed with A Hydroxamic Acid Inhibitor, PDB code: 1fm1: Calcium binding site 1 out of 1 in 1fm1Go back to![]() ![]()
Calcium binding site 1 out
of 1 in the Solution Structure of the Catalytic Fragment of Human Collagenase-3 (Mmp-13) Complexed with A Hydroxamic Acid Inhibitor
![]() Mono view ![]() Stereo pair view
Reference:
F.J.Moy,
P.K.Chanda,
J.M.Chen,
S.Cosmi,
W.Edris,
J.I.Levin,
R.Powers.
High-Resolution Solution Structure of the Catalytic Fragment of Human Collagenase-3 (Mmp-13) Complexed with A Hydroxamic Acid Inhibitor. J.Mol.Biol. V. 302 671 2000.
Page generated: Mon Jul 7 14:55:20 2025
ISSN: ISSN 0022-2836 PubMed: 10986126 DOI: 10.1006/JMBI.2000.4082 |
Last articlesCl in 8DGZCl in 8DDY Cl in 8DG6 Cl in 8DEO Cl in 8DE3 Cl in 8DE4 Cl in 8DCW Cl in 8DCT Cl in 8DCU Cl in 8DCV |
© Copyright 2008-2020 by atomistry.com | ||
Home | Site Map | Copyright | Contact us | Privacy |