Zinc in PDB 2k2g: Solution Structure of the Wild-Type Catalytic Domain of Human Matrix Metalloproteinase 12 (Mmp-12) in Complex with A Tight-Binding Inhibitor

All present enzymatic activity of Solution Structure of the Wild-Type Catalytic Domain of Human Matrix Metalloproteinase 12 (Mmp-12) in Complex with A Tight-Binding Inhibitor:
3.4.24.65;

The binding sites of Zinc atom in the Solution Structure of the Wild-Type Catalytic Domain of Human Matrix Metalloproteinase 12 (Mmp-12) in Complex with A Tight-Binding Inhibitor (pdb code 2k2g). 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 Wild-Type Catalytic Domain of Human Matrix Metalloproteinase 12 (Mmp-12) in Complex with A Tight-Binding Inhibitor, PDB code: 2k2g:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Solution Structure of the Wild-Type Catalytic Domain of Human Matrix Metalloproteinase 12 (Mmp-12) in Complex with A Tight-Binding Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Solution Structure of the Wild-Type Catalytic Domain of Human Matrix Metalloproteinase 12 (Mmp-12) in Complex with A Tight-Binding Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn2 b:0.0 occ:1.00 HE2 A:HIS222 1.1 0.0 1.0 HE2 A:HIS218 1.6 0.0 1.0 HE2 A:HIS228 1.8 0.0 1.0 NE2 A:HIS222 2.0 0.0 1.0 NE2 A:HIS218 2.2 0.0 1.0 NE2 A:HIS228 2.3 0.0 1.0 O40 A:DSV1 2.4 20.0 1.0 CE1 A:HIS228 2.9 0.0 1.0 CE1 A:HIS218 3.0 0.0 1.0 CE1 A:HIS222 3.0 0.0 1.0 CD2 A:HIS222 3.0 0.0 1.0 HE1 A:HIS228 3.1 0.0 1.0 HE1 A:HIS218 3.1 0.0 1.0 CD2 A:HIS218 3.2 0.0 1.0 HE1 A:HIS222 3.2 0.0 1.0 HD2 A:HIS222 3.3 0.0 1.0 CD2 A:HIS228 3.3 0.0 1.0 HD2 A:HIS218 3.6 0.0 1.0 C37 A:DSV1 3.6 20.0 1.0 HD2 A:HIS228 3.7 0.0 1.0 HG3 A:MET236 3.7 0.0 1.0 HG2 A:MET236 3.8 0.0 1.0 ND1 A:HIS228 4.0 0.0 1.0 ND1 A:HIS218 4.1 0.0 1.0 ND1 A:HIS222 4.1 0.0 1.0 CG A:HIS222 4.1 0.0 1.0 O39 A:DSV1 4.2 20.0 1.0 CG A:HIS228 4.2 0.0 1.0 CG A:MET236 4.2 0.0 1.0 CG A:HIS218 4.2 0.0 1.0 HB2 A:MET236 4.4 0.0 1.0 H6 A:DSV1 4.7 20.0 1.0 O A:HIS218 4.7 0.0 1.0 C10 A:DSV1 4.7 20.0 1.0 HD1 A:HIS228 4.8 0.0 1.0 N24 A:DSV1 4.8 20.0 1.0 CB A:MET236 4.9 0.0 1.0 H10 A:DSV1 4.9 20.0 1.0 HD1 A:HIS218 4.9 0.0 1.0 HA A:MET236 4.9 0.0 1.0 HD1 A:HIS222 5.0 0.0 1.0

Zinc binding site 2 out of 2 in the Solution Structure of the Wild-Type Catalytic Domain of Human Matrix Metalloproteinase 12 (Mmp-12) in Complex with A Tight-Binding Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Solution Structure of the Wild-Type Catalytic Domain of Human Matrix Metalloproteinase 12 (Mmp-12) in Complex with A Tight-Binding Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn3 b:0.0 occ:1.00 HE2 A:HIS183 1.3 0.0 1.0 HE2 A:HIS168 1.4 0.0 1.0 HB2 A:HIS196 1.7 0.0 1.0 HD1 A:HIS196 2.0 0.0 1.0 NE2 A:HIS183 2.2 0.0 1.0 ND1 A:HIS196 2.2 0.0 1.0 NE2 A:HIS168 2.2 0.0 1.0 CG A:HIS196 2.4 0.0 1.0 CB A:HIS196 2.4 0.0 1.0 CE1 A:HIS183 3.0 0.0 1.0 HE1 A:HIS183 3.1 0.0 1.0 CD2 A:HIS168 3.2 0.0 1.0 CE1 A:HIS168 3.2 0.0 1.0 HD1 A:PHE171 3.2 0.0 1.0 HB3 A:HIS196 3.2 0.0 1.0 CE1 A:HIS196 3.2 0.0 1.0 CD2 A:HIS183 3.3 0.0 1.0 H A:HIS196 3.3 0.0 1.0 CA A:HIS196 3.3 0.0 1.0 HZ A:PHE174 3.3 0.0 1.0 N A:HIS196 3.4 0.0 1.0 HD2 A:HIS168 3.4 0.0 1.0 CD1 A:PHE171 3.4 0.0 1.0 HE1 A:HIS168 3.4 0.0 1.0 CD2 A:HIS196 3.5 0.0 1.0 HE1 A:PHE171 3.5 0.0 1.0 HE1 A:PHE174 3.5 0.0 1.0 CE1 A:PHE171 3.6 0.0 1.0 HD2 A:HIS183 3.6 0.0 1.0 O A:HIS196 3.7 0.0 1.0 HB2 A:ASP170 3.7 0.0 1.0 C A:HIS196 3.8 0.0 1.0 HE1 A:HIS196 3.9 0.0 1.0 NE2 A:HIS196 3.9 0.0 1.0 CZ A:PHE174 4.1 0.0 1.0 ND1 A:HIS183 4.2 0.0 1.0 CE1 A:PHE174 4.2 0.0 1.0 HD2 A:HIS196 4.2 0.0 1.0 CG A:PHE171 4.2 0.0 1.0 HB2 A:PHE171 4.3 0.0 1.0 HA A:HIS196 4.3 0.0 1.0 C A:ALA195 4.3 0.0 1.0 CG A:HIS183 4.3 0.0 1.0 ND1 A:HIS168 4.3 0.0 1.0 CG A:HIS168 4.3 0.0 1.0 HA A:ALA195 4.4 0.0 1.0 CZ A:PHE171 4.5 0.0 1.0 CB A:ASP170 4.7 0.0 1.0 HB3 A:ASP170 4.7 0.0 1.0 HE2 A:HIS196 4.8 0.0 1.0 CB A:PHE171 4.8 0.0 1.0 N A:PHE197 4.8 0.0 1.0 O A:ALA195 4.9 0.0 1.0 CA A:ALA195 5.0 0.0 1.0 HZ A:PHE171 5.0 0.0 1.0 HD1 A:HIS183 5.0 0.0 1.0

M.A.Markus, B.Dwyer, S.Wolfrom, J.Li, W.Li, K.Malakian, J.Wilhelm, D.H.Tsao. Solution Structure of Wild-Type Human Matrix Metalloproteinase 12 (Mmp-12) in Complex with A Tight-Binding Inhibitor. J.Biomol.uc(Nmr) V. 41 55 2008.
ISSN: ISSN 0925-2738
PubMed: 18425585
DOI: 10.1007/S10858-008-9236-4