Zinc in PDB 1g12: 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: 1g12 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)	38.30 / 1.60
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	43.631, 41.757, 76.941, 90.00, 95.48, 90.00
R / Rfree (%)	21.8 / 22.9

The binding sites of Zinc atom in the Zinc Peptidase From Grifola Frondosa (pdb code 1g12). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Zinc Peptidase From Grifola Frondosa, PDB code: 1g12:

Zinc binding site 1 out of 1 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:11.6 occ:1.00 NE2 A:HIS117 2.0 10.1 1.0 NE2 A:HIS121 2.1 8.9 1.0 OD1 A:ASP130 2.1 12.6 1.0 O A:HOH401 2.3 15.7 1.0 O A:HOH754 2.3 27.7 1.0 OD2 A:ASP130 2.5 13.4 1.0 CG A:ASP130 2.6 12.7 1.0 CE1 A:HIS117 3.0 10.2 1.0 CD2 A:HIS117 3.0 10.0 1.0 CE1 A:HIS121 3.0 8.8 1.0 CD2 A:HIS121 3.1 8.7 1.0 CB A:ALA153 4.0 8.8 1.0 CB A:ASP130 4.1 12.6 1.0 ND1 A:HIS117 4.1 9.9 1.0 CG A:HIS117 4.2 10.0 1.0 ND1 A:HIS121 4.2 8.7 1.0 CG A:HIS121 4.3 8.7 1.0 OE2 A:GLU118 4.3 12.9 1.0 CE2 A:TYR133 4.3 16.0 1.0 OH A:TYR133 4.4 16.6 1.0 O A:HOH210 4.4 12.0 1.0 O A:HOH227 4.5 13.5 1.0 O A:HOH522 4.7 52.1 1.0 O A:HOH742 4.7 33.8 1.0 OE1 A:GLU118 4.7 12.4 1.0 CD A:GLU118 4.8 12.1 1.0 CZ A:TYR133 4.8 16.1 1.0 O A:HOH405 4.9 19.9 1.0 CA A:ASP130 4.9 12.5 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