Zinc in PDB 3hbv: Prtc Methionine Mutants: M226A in-House

The structure of Prtc Methionine Mutants: M226A in-House, PDB code: 3hbv was solved by A.E.Oberholzer, M.Bumann, T.Hege, S.Russo, U.Baumann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.35 / 1.95
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	101.961, 101.961, 123.222, 90.00, 90.00, 120.00
R / Rfree (%)	15.3 / 16.6

The structure of Prtc Methionine Mutants: M226A in-House also contains other interesting chemical elements:

Chlorine	(Cl)	4 atoms
Calcium	(Ca)	7 atoms

The binding sites of Zinc atom in the Prtc Methionine Mutants: M226A in-House (pdb code 3hbv). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Prtc Methionine Mutants: M226A in-House, PDB code: 3hbv:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Prtc Methionine Mutants: M226A in-House


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Prtc Methionine Mutants: M226A in-House within 5.0Å range: probe atom residue distance (Å) B Occ P:Zn486 b:38.7 occ:1.00 ND1 P:HIS198 2.1 44.5 1.0 O P:HOH960 2.1 37.4 1.0 NE2 P:HIS188 2.2 36.8 1.0 NE2 P:HIS192 2.2 41.0 1.0 CE1 P:HIS192 2.5 43.2 1.0 CE1 P:HIS198 3.0 43.1 1.0 CD2 P:HIS188 3.1 30.5 1.0 CE1 P:HIS188 3.2 40.5 1.0 CG P:HIS198 3.2 47.1 1.0 CD2 P:HIS192 3.4 43.0 1.0 CB P:HIS198 3.6 45.0 1.0 ND1 P:HIS192 3.8 44.1 1.0 NE2 P:HIS198 4.2 45.4 1.0 CG P:HIS192 4.2 38.4 1.0 CG P:HIS188 4.3 30.9 1.0 ND1 P:HIS188 4.3 35.7 1.0 CD2 P:HIS198 4.3 47.8 1.0 NE2 Z:GLN5 4.5 67.8 1.0 O P:HOH943 4.6 32.9 1.0 N P:HIS198 4.6 42.7 1.0 CA P:HIS198 4.7 44.3 1.0

Zinc binding site 2 out of 2 in the Prtc Methionine Mutants: M226A in-House


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Prtc Methionine Mutants: M226A in-House within 5.0Å range: probe atom residue distance (Å) B Occ P:Zn488 b:57.9 occ:1.00 OE2 P:GLU180 2.1 38.6 1.0 ND1 P:HIS241 2.2 41.4 1.0 O P:HOH746 2.4 25.5 1.0 O P:HOH899 2.4 52.0 1.0 CD P:GLU180 2.8 33.0 1.0 OE1 P:GLU180 2.9 29.4 1.0 CE1 P:HIS241 3.0 43.4 1.0 CG P:HIS241 3.3 39.2 1.0 CB P:HIS241 3.8 32.8 1.0 O P:HOH741 3.9 32.6 1.0 CB P:ALA290 4.0 36.5 1.0 NE2 P:HIS241 4.1 43.2 1.0 O P:ALA290 4.2 38.0 1.0 CG P:GLU180 4.3 24.8 1.0 CD2 P:HIS241 4.3 42.7 1.0 N P:ALA290 4.3 34.5 1.0 O P:HOH570 4.4 56.1 1.0 CA P:ALA290 4.6 33.9 1.0 CA P:HIS241 4.7 33.8 1.0 C P:ALA290 4.8 34.6 1.0 O P:HOH868 5.0 53.2 1.0

A.E.Oberholzer, M.Bumann, T.Hege, S.Russo, U.Baumann. Metzincin'S Canonical Methionine Is Responsible For the Structural Integrity of the Zinc-Binding Site Biol.Chem. V. 390 875 2009.
ISSN: ISSN 1431-6730
PubMed: 19558324
DOI: 10.1515/BC.2009.100