Zinc in PDB 1rm8: Crystal Structure of the Catalytic Domain of Mmp-16/MT3-Mmp: Characterization of Mt-Mmp Specific Features

The structure of Crystal Structure of the Catalytic Domain of Mmp-16/MT3-Mmp: Characterization of Mt-Mmp Specific Features, PDB code: 1rm8 was solved by R.Lang, M.Braun, N.E.Sounni, A.Noel, F.Frankenne, J.-M.Foidart, W.Bode, K.Maskos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	16.60 / 1.80
Space group	P 43 2 2
Cell size a, b, c (Å), α, β, γ (°)	51.210, 51.210, 149.368, 90.00, 90.00, 90.00
R / Rfree (%)	20.8 / 23.6

The structure of Crystal Structure of the Catalytic Domain of Mmp-16/MT3-Mmp: Characterization of Mt-Mmp Specific Features also contains other interesting chemical elements:

Calcium

(Ca)

2 atoms

The binding sites of Zinc atom in the Crystal Structure of the Catalytic Domain of Mmp-16/MT3-Mmp: Characterization of Mt-Mmp Specific Features (pdb code 1rm8). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the Catalytic Domain of Mmp-16/MT3-Mmp: Characterization of Mt-Mmp Specific Features, PDB code: 1rm8:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of the Catalytic Domain of Mmp-16/MT3-Mmp: Characterization of Mt-Mmp Specific Features


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Catalytic Domain of Mmp-16/MT3-Mmp: Characterization of Mt-Mmp Specific Features within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn500 b:17.2 occ:1.00 O1 A:BAT800 1.9 14.7 1.0 NE2 A:HIS250 2.0 13.7 1.0 NE2 A:HIS256 2.1 13.6 1.0 NE2 A:HIS246 2.2 18.1 1.0 O2 A:BAT800 2.2 14.1 1.0 C2 A:BAT800 2.8 15.8 1.0 N1 A:BAT800 2.9 13.1 1.0 CE1 A:HIS250 3.0 15.6 1.0 CD2 A:HIS256 3.0 15.1 1.0 CD2 A:HIS250 3.0 16.4 1.0 CE1 A:HIS246 3.1 16.5 1.0 CE1 A:HIS256 3.2 18.8 1.0 CD2 A:HIS246 3.2 16.8 1.0 ND1 A:HIS250 4.1 17.1 1.0 O A:HOH1000 4.2 18.0 1.0 CG A:HIS250 4.2 13.5 1.0 CG A:HIS256 4.2 17.1 1.0 C1 A:BAT800 4.2 15.5 1.0 ND1 A:HIS256 4.2 18.0 1.0 ND1 A:HIS246 4.2 14.3 1.0 C5 A:BAT800 4.3 19.6 1.0 CG A:HIS246 4.3 16.7 1.0 OE1 A:GLU247 4.4 19.9 1.0 OE2 A:GLU247 4.6 19.9 1.0 C9 A:BAT800 4.6 16.4 1.0 C6 A:BAT800 4.6 24.7 1.0 C8 A:BAT800 4.6 15.3 1.0 CD A:GLU247 4.8 16.5 1.0 C3 A:BAT800 4.9 17.1 1.0 CE A:MET264 4.9 14.8 1.0 C4 A:BAT800 4.9 21.9 1.0 O A:HOH1085 5.0 24.7 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the Catalytic Domain of Mmp-16/MT3-Mmp: Characterization of Mt-Mmp Specific Features


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the Catalytic Domain of Mmp-16/MT3-Mmp: Characterization of Mt-Mmp Specific Features within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:19.4 occ:1.00 OD2 A:ASP195 2.0 21.0 1.0 NE2 A:HIS193 2.0 18.6 1.0 ND1 A:HIS221 2.1 20.9 1.0 NE2 A:HIS208 2.2 19.3 0.5 NE2 A:HIS208 2.3 22.9 0.5 CE1 A:HIS208 2.6 19.1 0.5 CD2 A:HIS193 2.8 18.8 1.0 CG A:ASP195 2.9 17.0 1.0 CE1 A:HIS208 3.0 22.2 0.5 CE1 A:HIS221 3.1 18.0 1.0 OD1 A:ASP195 3.1 17.7 1.0 CE1 A:HIS193 3.2 21.4 1.0 CG A:HIS221 3.2 15.3 1.0 CD2 A:HIS208 3.3 19.4 0.5 CD2 A:HIS208 3.5 24.0 0.5 CB A:HIS221 3.5 16.4 1.0 ND1 A:HIS208 3.8 22.7 0.5 CG A:HIS193 4.0 17.8 1.0 ND1 A:HIS208 4.1 20.0 0.5 ND1 A:HIS193 4.2 18.7 1.0 NE2 A:HIS221 4.2 18.9 1.0 CG A:HIS208 4.3 17.2 0.5 CD2 A:HIS221 4.3 19.4 1.0 CG A:HIS208 4.3 16.2 0.5 O A:SER197 4.3 21.2 1.0 CB A:ASP195 4.3 21.6 1.0 OH A:TYR210 4.5 28.9 1.0 CB A:SER197 4.5 24.2 1.0 CZ A:PHE199 4.7 22.2 1.0 CE2 A:PHE199 4.8 24.0 1.0 CE1 A:TYR210 4.9 25.0 1.0 O A:HOH1001 4.9 19.6 1.0 C A:SER197 5.0 22.8 1.0

R.Lang, M.Braun, N.E.Sounni, A.Noel, F.Frankenne, J.M.Foidart, W.Bode, K.Maskos. Crystal Structure of the Catalytic Domain of Mmp-16/MT3-Mmp: Characterization of Mt-Mmp Specific Features. J.Mol.Biol. V. 336 213 2004.
ISSN: ISSN 0022-2836
PubMed: 14741217
DOI: 10.1016/J.JMB.2003.12.022