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Atomistry » Zinc » PDB 1f6u-1fp0 » 1fm1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 1f6u-1fp0 » 1fm1 » |
Zinc 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:
Zinc Binding Sites:
The binding sites of Zinc 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 Zinc atom.
In total 2 binding sites of Zinc where determined in the Solution Structure of the Catalytic Fragment of Human Collagenase-3 (Mmp-13) Complexed with A Hydroxamic Acid Inhibitor, PDB code: 1fm1: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 1fm1Go back to Zinc Binding Sites List in 1fm1
Zinc binding site 1 out
of 2 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
Zinc binding site 2 out of 2 in 1fm1Go back to Zinc Binding Sites List in 1fm1
Zinc binding site 2 out
of 2 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: Sun Oct 13 01:01:54 2024
ISSN: ISSN 0022-2836 PubMed: 10986126 DOI: 10.1006/JMBI.2000.4082 |
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