Zinc in PDB 1ge7: Zinc Peptidase From Grifola Frondosa

All present enzymatic activity of Zinc Peptidase From Grifola Frondosa:
3.4.24.20;

The structure of Zinc Peptidase From Grifola Frondosa, PDB code: 1ge7 was solved by T.Hori, T.Kumasaka, M.Yamamoto, T.Nonaka, N.Tanaka, Y.Hashimoto, T.Ueki, K.Takio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.00
Space group	P 43
Cell size a, b, c (Å), α, β, γ (°)	30.202, 30.202, 308.049, 90.00, 90.00, 90.00
R / Rfree (%)	17.9 / 21.8

The binding sites of Zinc atom in the Zinc Peptidase From Grifola Frondosa (pdb code 1ge7). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Zinc Peptidase From Grifola Frondosa, PDB code: 1ge7:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Zinc Peptidase From Grifola Frondosa


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Zinc Peptidase From Grifola Frondosa within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn200 b:15.4 occ:1.00 NE2 A:HIS121 2.0 11.9 1.0 NE2 A:HIS117 2.1 13.5 1.0 OD2 A:ASP130 2.1 15.5 1.0 O A:HOH393 2.1 24.3 1.0 OD1 A:ASP130 2.4 14.6 1.0 O A:HOH780 2.5 36.6 1.0 CG A:ASP130 2.6 14.3 1.0 CE1 A:HIS121 3.0 11.2 1.0 CD2 A:HIS121 3.1 11.8 1.0 CD2 A:HIS117 3.1 12.2 1.0 CE1 A:HIS117 3.1 13.0 1.0 CB A:ASP130 4.1 14.6 1.0 CB A:ALA153 4.1 11.7 1.0 OE2 A:GLU118 4.1 17.3 1.0 ND1 A:HIS121 4.2 11.5 1.0 CG A:HIS121 4.2 12.1 1.0 ND1 A:HIS117 4.2 13.1 1.0 CG A:HIS117 4.3 13.3 1.0 O A:HOH374 4.5 23.0 1.0 O A:HOH764 4.6 33.1 1.0 OE1 A:GLU118 4.6 16.1 1.0 O A:HOH370 4.7 17.0 1.0 CD A:GLU118 4.7 16.5 1.0 CA A:ASP130 5.0 14.5 1.0

Zinc binding site 2 out of 2 in the Zinc Peptidase From Grifola Frondosa


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Zinc Peptidase From Grifola Frondosa within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn200 b:16.3 occ:1.00 NE2 B:HIS117 2.0 12.9 1.0 NE2 B:HIS121 2.0 15.4 1.0 O B:HOH321 2.1 17.2 1.0 OD2 B:ASP130 2.2 15.8 1.0 OD1 B:ASP130 2.3 15.3 1.0 CG B:ASP130 2.6 15.1 1.0 CE1 B:HIS117 2.9 12.5 1.0 CE1 B:HIS121 3.0 14.8 1.0 CD2 B:HIS117 3.0 11.9 1.0 CD2 B:HIS121 3.1 14.4 1.0 OE2 B:GLU118 4.0 17.2 1.0 CB B:ALA153 4.1 14.0 1.0 ND1 B:HIS117 4.1 12.4 1.0 CB B:ASP130 4.1 15.7 1.0 CG B:HIS117 4.2 12.9 1.0 ND1 B:HIS121 4.2 15.0 1.0 CG B:HIS121 4.2 14.6 1.0 O B:HOH320 4.5 16.3 1.0 OE1 B:GLU118 4.5 15.8 1.0 O B:HOH323 4.6 11.8 1.0 CD B:GLU118 4.6 15.1 1.0

T.Hori, T.Kumasaka, M.Yamamoto, N.Nonaka, N.Tanaka, Y.Hashimoto, U.Ueki, K.Takio. Structure of A New 'Aspzincin' Metalloendopeptidase From Grifola Frondosa: Implications For the Catalytic Mechanism and Substrate Specificity Based on Several Different Crystal Forms. Acta Crystallogr.,Sect.D V. 57 361 2001.
ISSN: ISSN 0907-4449
PubMed: 11223512
DOI: 10.1107/S0907444900019740