Calcium in PDB 1i73: Complex of Pro-Leu-L-Trp Phosphonate with the Catalitic Domain of Matrix Metallo Proteinase-8 (MET80 Form)

All present enzymatic activity of Complex of Pro-Leu-L-Trp Phosphonate with the Catalitic Domain of Matrix Metallo Proteinase-8 (MET80 Form):
3.4.24.34;

The structure of Complex of Pro-Leu-L-Trp Phosphonate with the Catalitic Domain of Matrix Metallo Proteinase-8 (MET80 Form), PDB code: 1i73 was solved by E.Gavuzzo, G.Pochetti, F.Mazza, C.Gallina, B.Gorini, S.D'alessio, M.Pieper, H.Tschesche, P.A.Tucker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	32.983, 68.673, 70.486, 90.00, 90.00, 90.00
R / Rfree (%)	13.4 / 19.4

The structure of Complex of Pro-Leu-L-Trp Phosphonate with the Catalitic Domain of Matrix Metallo Proteinase-8 (MET80 Form) also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Calcium atom in the Complex of Pro-Leu-L-Trp Phosphonate with the Catalitic Domain of Matrix Metallo Proteinase-8 (MET80 Form) (pdb code 1i73). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Complex of Pro-Leu-L-Trp Phosphonate with the Catalitic Domain of Matrix Metallo Proteinase-8 (MET80 Form), PDB code: 1i73:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Complex of Pro-Leu-L-Trp Phosphonate with the Catalitic Domain of Matrix Metallo Proteinase-8 (MET80 Form)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Complex of Pro-Leu-L-Trp Phosphonate with the Catalitic Domain of Matrix Metallo Proteinase-8 (MET80 Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca996 b:8.9 occ:1.00 O A:GLY169 2.3 11.6 1.0 O A:GLY171 2.3 8.6 1.0 O A:ASP137 2.3 8.3 1.0 OD1 A:ASP173 2.4 9.4 1.0 O A:HOH402 2.4 11.5 1.0 O A:HOH397 2.4 9.1 1.0 CG A:ASP173 3.4 8.6 1.0 C A:ASP137 3.5 7.3 1.0 C A:GLY169 3.5 10.5 1.0 C A:GLY171 3.5 8.5 1.0 OD2 A:ASP173 3.8 9.3 1.0 C A:ILE170 3.9 8.9 1.0 N A:GLY171 3.9 9.1 1.0 O A:ILE170 4.1 8.6 1.0 N A:ASP173 4.2 7.0 1.0 CA A:ASP137 4.3 8.0 1.0 O A:ALA136 4.3 13.1 1.0 CA A:GLY171 4.3 9.2 1.0 N A:ILE170 4.4 12.2 1.0 CA A:ILE170 4.4 10.3 1.0 ND2 A:ASN139 4.4 20.0 1.0 O A:GLY167 4.4 11.8 1.0 N A:ILE138 4.4 8.3 1.0 CA A:GLY169 4.4 12.6 1.0 N A:GLY169 4.4 13.4 1.0 N A:GLY172 4.5 7.1 1.0 O A:HOH488 4.5 41.5 1.0 CA A:ILE138 4.5 6.4 1.0 CB A:ASP173 4.5 7.9 1.0 CA A:GLY172 4.6 7.8 1.0 C A:GLY172 4.7 7.3 1.0 O A:HOH407 4.7 13.2 1.0 N A:ASN139 4.8 8.6 1.0 CA A:ASP173 4.8 7.0 1.0 CH2 A:TRP88 4.8 11.3 1.0 C A:GLN168 4.8 13.0 1.0

Calcium binding site 2 out of 2 in the Complex of Pro-Leu-L-Trp Phosphonate with the Catalitic Domain of Matrix Metallo Proteinase-8 (MET80 Form)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Complex of Pro-Leu-L-Trp Phosphonate with the Catalitic Domain of Matrix Metallo Proteinase-8 (MET80 Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca997 b:7.6 occ:1.00 OE2 A:GLU180 2.3 10.2 1.0 O A:GLY155 2.3 9.5 1.0 O A:ILE159 2.3 8.9 1.0 OD2 A:ASP177 2.3 7.8 1.0 O A:ASN157 2.3 10.2 1.0 OD1 A:ASP154 2.3 8.8 1.0 CG A:ASP177 3.3 8.6 1.0 C A:ILE159 3.4 7.2 1.0 CD A:GLU180 3.5 10.2 1.0 C A:GLY155 3.5 9.6 1.0 CG A:ASP154 3.5 10.0 1.0 C A:ASN157 3.5 10.7 1.0 N A:ASN157 3.9 10.7 1.0 N A:ILE159 3.9 8.1 1.0 CB A:ASP177 3.9 6.7 1.0 N A:GLY155 4.0 10.2 1.0 C A:PRO156 4.1 10.8 1.0 OD2 A:ASP154 4.1 9.0 1.0 OE1 A:GLU180 4.2 11.3 1.0 CA A:ILE159 4.2 7.8 1.0 C A:ASP154 4.3 9.2 1.0 C A:GLY158 4.3 8.4 1.0 OD1 A:ASP177 4.3 8.1 1.0 CA A:ASN157 4.3 9.8 1.0 N A:ASP154 4.3 8.6 1.0 CA A:GLY155 4.4 10.0 1.0 N A:PRO156 4.4 10.8 1.0 N A:LEU160 4.4 6.6 1.0 CA A:PRO156 4.4 11.1 1.0 CG A:GLU180 4.5 8.9 1.0 N A:GLY158 4.5 9.8 1.0 O A:PRO156 4.5 12.0 1.0 CA A:LEU160 4.5 6.7 1.0 CA A:ASP154 4.6 9.2 1.0 CA A:GLY158 4.6 9.2 1.0 CB A:ASP154 4.6 7.9 1.0 CB A:ILE159 4.7 9.6 1.0 O A:ASP154 4.8 10.9 1.0 O A:GLY158 4.8 10.0 1.0

E.Gavuzzo, G.Pochetti, F.Mazza, C.Gallina, B.Gorini, S.D'alessio, M.Pieper, H.Tschesche, P.A.Tucker. Two Crystal Structures of Human Neutrophil Collagenase, One Complexed with A Primed- and the Other with An Unprimed-Side Inhibitor: Implications For Drug Design. J.Med.Chem. V. 43 3377 2000.
ISSN: ISSN 0022-2623
PubMed: 10978185
DOI: 10.1021/JM9909589