Calcium in PDB 1jan: Complex of Pro-Leu-Gly-Hydroxylamine with the Catalytic Domain of Matrix Metallo Proteinase-8 (PHE79 Form)

All present enzymatic activity of Complex of Pro-Leu-Gly-Hydroxylamine with the Catalytic Domain of Matrix Metallo Proteinase-8 (PHE79 Form):
3.4.24.34;

The structure of Complex of Pro-Leu-Gly-Hydroxylamine with the Catalytic Domain of Matrix Metallo Proteinase-8 (PHE79 Form), PDB code: 1jan was solved by P.Reinemer, F.Grams, R.Huber, T.Kleine, S.Schnierer, M.Pieper, H.Tschesche, W.Bode, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	33.210, 69.530, 72.540, 90.00, 90.00, 90.00
R / Rfree (%)	18 / n/a

The structure of Complex of Pro-Leu-Gly-Hydroxylamine with the Catalytic Domain of Matrix Metallo Proteinase-8 (PHE79 Form) also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Calcium atom in the Complex of Pro-Leu-Gly-Hydroxylamine with the Catalytic Domain of Matrix Metallo Proteinase-8 (PHE79 Form) (pdb code 1jan). 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-Gly-Hydroxylamine with the Catalytic Domain of Matrix Metallo Proteinase-8 (PHE79 Form), PDB code: 1jan:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Complex of Pro-Leu-Gly-Hydroxylamine with the Catalytic Domain of Matrix Metallo Proteinase-8 (PHE79 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-Gly-Hydroxylamine with the Catalytic Domain of Matrix Metallo Proteinase-8 (PHE79 Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca996 b:10.7 occ:1.00 H2 A:HOH1028 1.2 15.0 1.0 H1 A:HOH1027 1.8 15.0 1.0 O A:HOH1028 2.1 12.2 1.0 O A:ASP137 2.2 9.2 1.0 O A:GLY171 2.3 7.9 1.0 O A:GLY169 2.3 13.2 1.0 OD1 A:ASP173 2.4 11.1 1.0 O A:HOH1027 2.5 12.2 1.0 H1 A:HOH1028 2.6 15.0 1.0 H2 A:HOH1027 3.1 15.0 1.0 C A:ASP137 3.4 9.9 1.0 C A:GLY171 3.4 8.0 1.0 C A:GLY169 3.5 13.2 1.0 CG A:ASP173 3.5 12.2 1.0 HD22 A:ASN139 3.7 15.0 1.0 H A:ASP173 3.8 15.0 1.0 H2 A:HOH1045 3.9 15.0 1.0 N A:GLY171 4.0 6.1 1.0 H A:ASN139 4.0 15.0 1.0 C A:ILE170 4.0 7.7 1.0 OD2 A:ASP173 4.1 14.4 1.0 H A:GLY171 4.1 15.0 1.0 H A:GLY169 4.2 15.0 1.0 N A:ASP173 4.2 7.5 1.0 O A:ILE170 4.2 5.5 1.0 CA A:GLY171 4.3 7.1 1.0 N A:ILE138 4.3 7.8 1.0 CA A:ASP137 4.3 10.8 1.0 CA A:ILE138 4.3 6.4 1.0 N A:ILE170 4.4 11.2 1.0 O A:GLY167 4.4 15.4 1.0 N A:GLY169 4.4 14.7 1.0 CA A:ILE170 4.4 8.6 1.0 N A:GLY172 4.4 7.1 1.0 O A:ALA136 4.4 15.9 1.0 CA A:GLY169 4.5 12.4 1.0 CA A:GLY172 4.5 6.4 1.0 C A:GLY172 4.6 6.3 1.0 O A:HOH1045 4.6 8.2 1.0 ND2 A:ASN139 4.7 7.2 1.0 CB A:ASP173 4.7 9.4 1.0 N A:ASN139 4.7 6.6 1.0 CA A:ASP173 4.8 7.4 1.0 CH2 A:TRP88 4.9 12.8 1.0

Calcium binding site 2 out of 2 in the Complex of Pro-Leu-Gly-Hydroxylamine with the Catalytic Domain of Matrix Metallo Proteinase-8 (PHE79 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-Gly-Hydroxylamine with the Catalytic Domain of Matrix Metallo Proteinase-8 (PHE79 Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca997 b:10.9 occ:1.00 O A:GLY155 2.2 11.7 1.0 O A:ILE159 2.3 8.4 1.0 OD1 A:ASP154 2.3 5.9 1.0 OE2 A:GLU180 2.4 6.1 1.0 O A:ASN157 2.4 7.9 1.0 OD2 A:ASP177 2.4 14.4 1.0 CG A:ASP177 3.3 13.6 1.0 C A:GLY155 3.4 9.8 1.0 H A:ASP154 3.4 15.0 1.0 C A:ILE159 3.4 8.5 1.0 CG A:ASP154 3.5 8.1 1.0 C A:ASN157 3.6 6.4 1.0 CD A:GLU180 3.6 5.2 1.0 N A:GLY155 3.9 10.1 1.0 H A:GLY155 3.9 15.0 1.0 H A:ILE159 3.9 15.0 1.0 N A:ILE159 3.9 4.8 1.0 N A:ASN157 4.0 9.3 1.0 CB A:ASP177 4.0 13.4 1.0 C A:PRO156 4.0 9.8 1.0 OD2 A:ASP154 4.1 8.2 1.0 C A:ASP154 4.2 10.0 1.0 H A:ASN157 4.2 15.0 1.0 OD1 A:ASP177 4.2 10.2 1.0 CA A:ILE159 4.2 7.2 1.0 N A:ASP154 4.2 10.7 1.0 C A:GLY158 4.2 4.8 1.0 CA A:GLY155 4.3 9.4 1.0 CA A:ASN157 4.3 7.7 1.0 N A:PRO156 4.3 8.5 1.0 O A:PRO156 4.4 8.4 1.0 CA A:PRO156 4.4 8.3 1.0 CG A:GLU180 4.4 4.6 1.0 N A:LEU160 4.4 7.1 1.0 OE1 A:GLU180 4.4 3.9 1.0 N A:GLY158 4.5 4.8 1.0 CA A:ASP154 4.5 9.7 1.0 O A:ASP154 4.6 11.1 1.0 CA A:GLY158 4.6 4.1 1.0 CB A:ASP154 4.6 9.3 1.0 CG2 A:ILE159 4.7 11.8 1.0 CA A:LEU160 4.7 5.7 1.0 O A:GLY158 4.7 3.1 1.0 H2 A:HOH1020 4.9 15.0 1.0 CB A:ILE159 5.0 8.9 1.0

P.Reinemer, F.Grams, R.Huber, T.Kleine, S.Schnierer, M.Piper, H.Tschesche, W.Bode. Structural Implications For the Role of the N Terminus in the 'Superactivation' of Collagenases. A Crystallographic Study. Febs Lett. V. 338 227 1994.
ISSN: ISSN 0014-5793
PubMed: 8307185
DOI: 10.1016/0014-5793(94)80370-6