Zinc in PDB 2z58: Crystal Structure of G56W-Propeptide:S324A-Subtilisin Complex

All present enzymatic activity of Crystal Structure of G56W-Propeptide:S324A-Subtilisin Complex:
3.4.21.62;

The structure of Crystal Structure of G56W-Propeptide:S324A-Subtilisin Complex, PDB code: 2z58 was solved by M.A.Pulido, S.Tanaka, C.Sringiew, D.J.You, H.Matsumura, Y.Koga, K.Takano, S.Kanaya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.88
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	64.837, 67.345, 74.031, 90.00, 90.00, 90.00
R / Rfree (%)	19.5 / 22.6

The structure of Crystal Structure of G56W-Propeptide:S324A-Subtilisin Complex also contains other interesting chemical elements:

Calcium

(Ca)

7 atoms

The binding sites of Zinc atom in the Crystal Structure of G56W-Propeptide:S324A-Subtilisin Complex (pdb code 2z58). 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 Crystal Structure of G56W-Propeptide:S324A-Subtilisin Complex, PDB code: 2z58:

Zinc binding site 1 out of 1 in the Crystal Structure of G56W-Propeptide:S324A-Subtilisin Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of G56W-Propeptide:S324A-Subtilisin Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn263 b:31.3 occ:1.00 NE2 B:HIS28 2.0 29.8 1.0 OD2 B:ASP42 2.1 23.7 1.0 CE1 B:HIS28 2.7 33.4 1.0 CG B:ASP42 2.9 23.4 1.0 CD2 B:HIS28 3.2 30.3 1.0 CB B:ASP42 3.2 25.9 1.0 ND1 B:HIS28 3.9 30.9 1.0 OD1 B:ASP42 4.1 23.9 1.0 NH2 B:ARG7 4.1 23.8 1.0 CG B:HIS28 4.2 27.6 1.0 CG2 B:VAL30 4.6 25.4 1.0 O B:HOH272 4.6 39.9 1.0 CA B:ASP42 4.8 24.8 1.0

M.A.Pulido, S.Tanaka, C.Sringiew, D.J.You, H.Matsumura, Y.Koga, K.Takano, S.Kanaya. Requirement of Left-Handed Glycine Residue For High Stability of the Tk-Subtilisin Propeptide As Revealed By Mutational and Crystallographic Analyses J.Mol.Biol. V. 374 1359 2007.
ISSN: ISSN 0022-2836
PubMed: 17988685
DOI: 10.1016/J.JMB.2007.10.030