Zinc 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:

Calcium

(Ca)

2 atoms

The binding sites of Zinc 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 Zinc atom.
In total 2 binding sites of Zinc 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 Zinc binding site number: 1; 2;

Zinc 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 Zinc with other atoms in the Zn 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:Zn998 b:9.2 occ:1.00 OD2 A:ASP149 1.8 6.8 1.0 ND1 A:HIS175 2.0 6.7 1.0 NE2 A:HIS147 2.2 7.2 1.0 NE2 A:HIS162 2.3 9.7 1.0 CG A:ASP149 2.8 10.3 1.0 CD2 A:HIS147 2.9 5.4 1.0 CE1 A:HIS175 3.0 7.2 1.0 CG A:HIS175 3.1 3.5 1.0 CE1 A:HIS162 3.1 9.6 1.0 OD1 A:ASP149 3.3 10.8 1.0 CE1 A:HIS147 3.4 7.7 1.0 CD2 A:HIS162 3.4 11.2 1.0 CB A:HIS175 3.4 4.4 1.0 CB A:ASP149 4.1 9.8 1.0 NE2 A:HIS175 4.2 4.4 1.0 H2 A:HOH1025 4.2 15.0 1.0 CG A:HIS147 4.2 5.0 1.0 CD2 A:HIS175 4.2 4.5 1.0 CE1 A:PHE164 4.3 4.4 1.0 ND1 A:HIS162 4.3 9.5 1.0 CZ A:PHE164 4.4 4.2 1.0 ND1 A:HIS147 4.4 6.1 1.0 O A:SER151 4.4 10.3 1.0 CG A:HIS162 4.5 9.9 1.0 H1 A:HOH1076 4.6 15.0 1.0 CZ A:PHE153 4.7 5.5 1.0 H1 A:HOH1025 4.7 15.0 1.0 CE2 A:PHE153 4.7 7.3 1.0 H2 A:HOH1076 4.7 15.0 1.0 CA A:HIS175 4.9 5.6 1.0 H A:ASP149 4.9 15.0 1.0 O A:HOH1025 4.9 15.1 1.0

Zinc 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 Zinc with other atoms in the Zn 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:Zn999 b:7.4 occ:1.00 HO I:HOA4 1.2 15.0 1.0 NE2 A:HIS207 1.9 8.1 1.0 NE2 A:HIS197 2.0 5.5 1.0 O I:HOA4 2.1 11.4 1.0 NE2 A:HIS201 2.1 2.9 1.0 O I:GLY3 2.2 13.1 1.0 CE1 A:HIS207 2.7 7.8 1.0 C I:GLY3 2.9 10.3 1.0 N I:HOA4 2.9 9.0 1.0 CD2 A:HIS197 3.0 6.1 1.0 CD2 A:HIS207 3.0 7.8 1.0 CE1 A:HIS201 3.1 4.4 1.0 CE1 A:HIS197 3.1 6.9 1.0 CD2 A:HIS201 3.2 2.0 1.0 HN1 I:HOA4 3.8 15.0 1.0 ND1 A:HIS207 3.9 8.1 1.0 CG A:HIS207 4.0 8.5 1.0 H1 A:HOH1023 4.2 15.0 1.0 CG A:HIS197 4.2 7.2 1.0 ND1 A:HIS201 4.2 3.3 1.0 ND1 A:HIS197 4.2 6.8 1.0 H1 A:HOH1021 4.3 15.0 1.0 CG A:HIS201 4.3 2.7 1.0 O A:HOH1023 4.3 24.6 1.0 CA I:GLY3 4.3 11.4 1.0 OE2 A:GLU198 4.5 7.6 1.0 N I:GLY3 4.6 12.7 1.0 HD1 A:HIS207 4.7 15.0 1.0 OE1 A:GLU198 4.7 2.1 1.0 O I:LEU2 4.8 14.4 1.0 CE A:MET215 4.8 3.7 1.0 C I:LEU2 4.8 14.8 1.0 CD A:GLU198 5.0 4.9 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