Zinc in PDB 2n8r: Productive Complex Between Mmp-12 and Synthetic Triple-Helical Collagen, Revealed Through Paramagnetic uc(Nmr)

All present enzymatic activity of Productive Complex Between Mmp-12 and Synthetic Triple-Helical Collagen, Revealed Through Paramagnetic uc(Nmr):
3.4.24.65;

The structure of Productive Complex Between Mmp-12 and Synthetic Triple-Helical Collagen, Revealed Through Paramagnetic uc(Nmr) also contains other interesting chemical elements:

Calcium

(Ca)

3 atoms

The binding sites of Zinc atom in the Productive Complex Between Mmp-12 and Synthetic Triple-Helical Collagen, Revealed Through Paramagnetic uc(Nmr) (pdb code 2n8r). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Productive Complex Between Mmp-12 and Synthetic Triple-Helical Collagen, Revealed Through Paramagnetic uc(Nmr), PDB code: 2n8r:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Productive Complex Between Mmp-12 and Synthetic Triple-Helical Collagen, Revealed Through Paramagnetic uc(Nmr)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Productive Complex Between Mmp-12 and Synthetic Triple-Helical Collagen, Revealed Through Paramagnetic uc(Nmr) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:0.0 occ:1.00 O A:HOH401 1.9 0.0 1.0 O D:GLY88 1.9 0.0 1.0 O D:PRO87 2.1 0.0 1.0 NE2 A:HIS218 2.1 0.0 1.0 NE2 A:HIS222 2.1 0.0 1.0 NE2 A:HIS228 2.1 0.0 1.0 H1 A:HOH401 2.7 0.0 1.0 H2 A:HOH401 2.7 0.0 1.0 C D:GLY88 3.0 0.0 1.0 CE1 A:HIS228 3.0 0.0 1.0 CD2 A:HIS222 3.1 0.0 1.0 CE1 A:HIS218 3.1 0.0 1.0 C D:PRO87 3.1 0.0 1.0 CD2 A:HIS218 3.2 0.0 1.0 CE1 A:HIS222 3.2 0.0 1.0 HE1 A:HIS228 3.2 0.0 1.0 CD2 A:HIS228 3.2 0.0 1.0 HD2 A:HIS222 3.3 0.0 1.0 HE1 A:HIS218 3.4 0.0 1.0 HD2 A:HIS218 3.4 0.0 1.0 HE1 A:HIS222 3.5 0.0 1.0 HA2 D:GLY88 3.5 0.0 1.0 CA D:GLY88 3.6 0.0 1.0 HD2 A:HIS228 3.6 0.0 1.0 HB D:VAL89 3.6 0.0 1.0 N D:GLY88 3.7 0.0 1.0 HG12 D:VAL89 3.9 0.0 1.0 OE2 A:GLU219 4.0 0.0 1.0 N D:VAL89 4.1 0.0 1.0 HE3 A:MET236 4.1 0.0 1.0 ND1 A:HIS228 4.2 0.0 1.0 ND1 A:HIS218 4.2 0.0 1.0 CG A:HIS222 4.2 0.0 1.0 CG A:HIS218 4.3 0.0 1.0 CG A:HIS228 4.3 0.0 1.0 ND1 A:HIS222 4.3 0.0 1.0 CB D:VAL89 4.4 0.0 1.0 HE1 A:MET236 4.4 0.0 1.0 CA D:PRO87 4.4 0.0 1.0 CG1 D:VAL89 4.5 0.0 1.0 HB2 C:PRO51 4.5 0.0 1.0 O C:GLY52 4.6 0.0 1.0 HA3 D:GLY88 4.6 0.0 1.0 H D:GLY88 4.7 0.0 1.0 CA D:VAL89 4.7 0.0 1.0 HG11 D:VAL89 4.7 0.0 1.0 H C:GLY52 4.7 0.0 1.0 CE A:MET236 4.8 0.0 1.0 N D:PRO87 4.8 0.0 1.0 HA A:PRO238 4.8 0.0 1.0 HB2 D:PRO87 4.8 0.0 1.0 HA D:VAL89 4.9 0.0 1.0 H D:VAL89 4.9 0.0 1.0 O D:PRO86 4.9 0.0 1.0 CD A:GLU219 4.9 0.0 1.0

Zinc binding site 2 out of 2 in the Productive Complex Between Mmp-12 and Synthetic Triple-Helical Collagen, Revealed Through Paramagnetic uc(Nmr)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Productive Complex Between Mmp-12 and Synthetic Triple-Helical Collagen, Revealed Through Paramagnetic uc(Nmr) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:0.0 occ:1.00 OD1 A:ASP170 1.8 0.0 1.0 NE2 A:HIS168 2.1 0.0 1.0 NE2 A:HIS183 2.1 0.0 1.0 ND1 A:HIS196 2.1 0.0 1.0 OD2 A:ASP170 2.1 0.0 1.0 CG A:ASP170 2.4 0.0 1.0 CE1 A:HIS196 2.9 0.0 1.0 CD2 A:HIS168 2.9 0.0 1.0 CE1 A:HIS183 3.0 0.0 1.0 HE1 A:HIS196 3.0 0.0 1.0 CE1 A:HIS168 3.1 0.0 1.0 HE1 A:HIS183 3.1 0.0 1.0 HD2 A:HIS168 3.2 0.0 1.0 CD2 A:HIS183 3.3 0.0 1.0 CG A:HIS196 3.3 0.0 1.0 HE1 A:HIS168 3.5 0.0 1.0 HD2 A:HIS183 3.6 0.0 1.0 HB2 A:HIS172 3.7 0.0 1.0 HB2 A:HIS196 3.7 0.0 1.0 CB A:ASP170 3.8 0.0 1.0 HB3 A:HIS196 3.9 0.0 1.0 CG A:HIS168 3.9 0.0 1.0 CB A:HIS196 3.9 0.0 1.0 ND1 A:HIS168 4.0 0.0 1.0 NE2 A:HIS196 4.1 0.0 1.0 ND1 A:HIS183 4.2 0.0 1.0 HB3 A:ASP170 4.2 0.0 1.0 H A:ASP170 4.2 0.0 1.0 O A:HIS168 4.3 0.0 1.0 CD2 A:HIS196 4.3 0.0 1.0 HE2 A:PHE185 4.3 0.0 1.0 CG A:HIS183 4.3 0.0 1.0 N A:ASP170 4.4 0.0 1.0 HB2 A:ASP170 4.5 0.0 1.0 HD2 A:HIS172 4.5 0.0 1.0 CA A:ASP170 4.6 0.0 1.0 CB A:HIS172 4.7 0.0 1.0 CE2 A:PHE185 4.8 0.0 1.0 C A:HIS168 4.9 0.0 1.0 HD1 A:HIS168 4.9 0.0 1.0 H A:HIS172 5.0 0.0 1.0 HE2 A:HIS196 5.0 0.0 1.0

S.H.Prior, T.S.Byrne, D.Tokmina-Roszyk, G.B.Fields, S.R.Van Doren. Path to Collagenolysis: Collagen V Triple-Helix Model Bound Productively and in Encounters By Matrix Metalloproteinase-12. J.Biol.Chem. V. 291 7888 2016.
ISSN: ISSN 0021-9258
PubMed: 26887942
DOI: 10.1074/JBC.M115.703124