Zinc in PDB 3hbu: Prtc Methionine Mutants: M226H Desy

The structure of Prtc Methionine Mutants: M226H Desy, PDB code: 3hbu 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)	37.16 / 1.77
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	102.112, 102.112, 122.863, 90.00, 90.00, 120.00
R / Rfree (%)	16.6 / 18.7

The structure of Prtc Methionine Mutants: M226H Desy also contains other interesting chemical elements:

Chlorine	(Cl)	2 atoms
Calcium	(Ca)	7 atoms

The binding sites of Zinc atom in the Prtc Methionine Mutants: M226H Desy (pdb code 3hbu). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Prtc Methionine Mutants: M226H Desy, PDB code: 3hbu:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Prtc Methionine Mutants: M226H Desy


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: M226H Desy within 5.0Å range: probe atom residue distance (Å) B Occ P:Zn486 b:23.5 occ:0.50 NE2 P:HIS198 2.0 63.9 1.0 CE1 P:HIS198 2.0 61.0 1.0 NE2 P:HIS188 2.1 22.9 0.5 NE2 P:HIS192 2.2 54.3 1.0 O Z:HOH436 2.2 31.5 1.0 CD2 P:HIS192 2.7 52.1 1.0 CE1 P:HIS188 3.1 21.6 0.5 CD2 P:HIS188 3.1 26.6 0.5 ND1 P:HIS198 3.3 66.3 1.0 CD2 P:HIS198 3.3 62.2 1.0 O Z:ALA4 3.3 65.8 1.0 NE2 P:HIS188 3.3 32.8 0.5 CE1 P:HIS192 3.4 47.7 1.0 ZN P:ZN487 3.5 28.8 0.5 CE1 P:HIS188 3.6 26.7 0.5 CG P:HIS198 3.9 61.0 1.0 CB Z:ALA3 3.9 49.2 1.0 CD2 P:HIS188 4.0 21.0 0.5 CG P:HIS192 4.0 39.5 1.0 C Z:ALA3 4.1 46.9 1.0 O Z:ALA3 4.1 29.7 1.0 O P:HOH849 4.1 47.0 1.0 C Z:ALA4 4.2 60.8 1.0 ND1 P:HIS188 4.2 22.6 0.5 CG P:HIS188 4.2 21.7 0.5 ND1 P:HIS192 4.3 48.1 1.0 N Z:ALA4 4.3 46.6 1.0 ND1 P:HIS188 4.3 22.8 0.5 CG P:HIS188 4.5 20.2 0.5 CA Z:ALA3 4.6 51.4 1.0 CA Z:ALA4 4.7 56.2 1.0

Zinc binding site 2 out of 3 in the Prtc Methionine Mutants: M226H Desy


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: M226H Desy within 5.0Å range: probe atom residue distance (Å) B Occ P:Zn487 b:28.8 occ:0.50 CD2 P:HIS198 1.6 62.2 1.0 CE1 P:HIS192 2.0 47.7 1.0 NE2 P:HIS188 2.0 32.8 0.5 NE2 P:HIS198 2.1 63.9 1.0 NE2 P:HIS192 2.2 54.3 1.0 CB P:HIS226 2.7 41.1 1.0 CG P:HIS198 2.7 61.0 1.0 CD2 P:HIS188 2.9 21.0 0.5 ND1 P:HIS226 3.0 44.0 1.0 O P:HIS226 3.0 36.4 1.0 CE1 P:HIS188 3.0 26.7 0.5 CA P:HIS226 3.1 38.6 1.0 ND1 P:HIS192 3.2 48.1 1.0 NE2 P:HIS188 3.2 22.9 0.5 CE1 P:HIS198 3.2 61.0 1.0 CG P:HIS226 3.2 44.6 1.0 ZN P:ZN486 3.5 23.5 0.5 C P:HIS226 3.5 39.9 1.0 CD2 P:HIS192 3.5 52.1 1.0 ND1 P:HIS198 3.5 66.3 1.0 CE1 P:HIS188 3.5 21.6 0.5 CA P:HIS198 3.6 52.6 1.0 N P:HIS198 3.7 52.7 1.0 CB P:HIS198 3.7 59.8 1.0 CD2 P:HIS188 3.9 26.6 0.5 CG P:HIS192 4.0 39.5 1.0 CG P:HIS188 4.1 20.2 0.5 ND1 P:HIS188 4.1 22.8 0.5 C P:ALA197 4.3 49.5 1.0 CE1 P:HIS226 4.3 28.1 1.0 ND1 P:HIS188 4.3 22.6 0.5 N P:HIS226 4.5 32.5 1.0 CG P:HIS188 4.5 21.7 0.5 CD2 P:HIS226 4.6 38.8 1.0 O P:ALA197 4.6 56.8 1.0 N P:SER227 4.8 43.9 1.0 CD P:PRO199 4.9 50.0 1.0 C P:HIS198 5.0 45.7 1.0

Zinc binding site 3 out of 3 in the Prtc Methionine Mutants: M226H Desy


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Prtc Methionine Mutants: M226H Desy within 5.0Å range: probe atom residue distance (Å) B Occ P:Zn488 b:66.9 occ:1.00 OE2 P:GLU180 2.1 37.1 1.0 ND1 P:HIS241 2.4 33.3 1.0 O P:HOH687 2.5 26.1 1.0 CD P:GLU180 2.8 33.0 1.0 OE1 P:GLU180 2.9 32.3 1.0 CE1 P:HIS241 3.0 36.8 1.0 CG P:HIS241 3.3 33.2 1.0 O P:HOH958 3.7 33.3 1.0 CB P:HIS241 3.8 26.1 1.0 CB P:ALA290 3.9 26.3 1.0 NE2 P:HIS241 4.0 33.1 1.0 O P:ALA290 4.2 37.8 1.0 CD2 P:HIS241 4.2 34.8 1.0 CG P:GLU180 4.2 20.3 1.0 N P:ALA290 4.4 27.6 1.0 O P:HOH707 4.4 41.5 1.0 CA P:ALA290 4.6 24.6 1.0 C P:ALA290 4.8 30.7 1.0 CA P:HIS241 4.8 27.4 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