Zinc in PDB 7zbh: Atp-Dependent Zinc Metalloprotease Ftsh (BB0789) From Borrelia Burgdorferi

The structure of Atp-Dependent Zinc Metalloprotease Ftsh (BB0789) From Borrelia Burgdorferi, PDB code: 7zbh was solved by K.Brangulis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	96.75 / 3.30
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	153.81, 192.8, 114.13, 90, 124.31, 90
R / Rfree (%)	27.9 / 33.2

The binding sites of Zinc atom in the Atp-Dependent Zinc Metalloprotease Ftsh (BB0789) From Borrelia Burgdorferi (pdb code 7zbh). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the Atp-Dependent Zinc Metalloprotease Ftsh (BB0789) From Borrelia Burgdorferi, PDB code: 7zbh:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6;

Zinc binding site 1 out of 6 in the Atp-Dependent Zinc Metalloprotease Ftsh (BB0789) From Borrelia Burgdorferi


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Atp-Dependent Zinc Metalloprotease Ftsh (BB0789) From Borrelia Burgdorferi within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn702 b:66.9 occ:0.00 NE2 A:HIS434 1.2 71.9 1.0 OD2 A:ASP510 1.6 76.0 1.0 NE2 A:HIS438 1.7 107.0 1.0 CE1 A:HIS434 1.9 76.1 1.0 CG A:ASP510 2.2 79.7 1.0 CD2 A:HIS434 2.3 106.0 1.0 OD1 A:ASP510 2.4 110.3 1.0 CE1 A:HIS438 2.6 110.0 1.0 CD2 A:HIS438 2.8 120.0 1.0 ND1 A:HIS434 3.0 88.6 1.0 CG A:HIS434 3.2 105.8 1.0 CB A:ASP510 3.5 95.7 1.0 ND1 A:HIS438 3.7 132.7 1.0 CG A:HIS438 3.9 134.8 1.0 O A:GLY506 4.3 93.5 1.0 CB A:HIS434 4.6 104.8 1.0 CA A:ASP510 4.8 99.1 1.0 O A:CYS489 4.8 65.0 1.0 OE2 A:GLU435 4.8 86.9 1.0 O A:HIS434 4.8 151.2 1.0 CA A:GLY492 5.0 80.7 1.0

Zinc binding site 2 out of 6 in the Atp-Dependent Zinc Metalloprotease Ftsh (BB0789) From Borrelia Burgdorferi


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Atp-Dependent Zinc Metalloprotease Ftsh (BB0789) From Borrelia Burgdorferi within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn702 b:77.7 occ:0.00 NE2 B:HIS438 1.7 97.4 1.0 OD2 B:ASP510 1.7 116.3 1.0 NE2 B:HIS434 1.9 96.3 1.0 CD2 B:HIS438 2.5 115.9 1.0 CD2 B:HIS434 2.7 106.4 1.0 CG B:ASP510 2.7 123.3 1.0 CE1 B:HIS438 2.8 104.3 1.0 CE1 B:HIS434 3.0 115.4 1.0 OD1 B:ASP510 3.0 124.7 1.0 CG B:HIS438 3.6 138.8 1.0 ND1 B:HIS438 3.7 125.1 1.0 CG B:HIS434 3.9 122.1 1.0 ND1 B:HIS434 4.0 115.7 1.0 CB B:ASP510 4.1 121.9 1.0 OE2 B:GLU435 4.5 97.0 1.0 OE1 B:GLU435 4.5 113.6 1.0 CD B:GLU435 4.9 110.9 1.0 CB B:HIS438 5.0 128.5 1.0 O B:GLY506 5.0 91.3 1.0

Zinc binding site 3 out of 6 in the Atp-Dependent Zinc Metalloprotease Ftsh (BB0789) From Borrelia Burgdorferi


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Atp-Dependent Zinc Metalloprotease Ftsh (BB0789) From Borrelia Burgdorferi within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn702 b:79.3 occ:0.00 NE2 D:HIS438 1.9 95.9 1.0 NE2 D:HIS434 2.0 73.0 1.0 OD2 D:ASP510 2.1 91.1 1.0 CD2 D:HIS438 2.5 125.0 1.0 CD2 D:HIS434 2.6 85.5 1.0 CE1 D:HIS438 3.0 135.1 1.0 CG D:ASP510 3.1 102.6 1.0 CE1 D:HIS434 3.2 91.0 1.0 OD1 D:ASP510 3.3 125.1 1.0 CG D:HIS438 3.6 138.8 1.0 ND1 D:HIS438 3.8 144.9 1.0 CG D:HIS434 3.9 106.4 1.0 OE2 D:GLU435 4.1 128.1 1.0 ND1 D:HIS434 4.1 116.7 1.0 OE1 D:GLU435 4.2 154.0 1.0 CB D:ASP510 4.5 119.5 1.0 CD D:GLU435 4.5 157.9 1.0 CB D:HIS438 4.9 129.1 1.0

Zinc binding site 4 out of 6 in the Atp-Dependent Zinc Metalloprotease Ftsh (BB0789) From Borrelia Burgdorferi


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Atp-Dependent Zinc Metalloprotease Ftsh (BB0789) From Borrelia Burgdorferi within 5.0Å range: probe atom residue distance (Å) B Occ F:Zn702 b:79.2 occ:0.00 NE2 F:HIS434 2.2 79.2 1.0 OD2 F:ASP510 2.6 82.9 1.0 NE2 F:HIS438 2.8 99.3 1.0 CD2 F:HIS434 2.8 101.4 1.0 OD1 F:ASP510 3.2 121.0 1.0 CG F:ASP510 3.3 91.1 1.0 CD2 F:HIS438 3.3 109.6 1.0 CE1 F:HIS434 3.4 79.0 1.0 CE1 F:HIS438 3.9 93.2 1.0 OE2 F:GLU435 4.0 77.2 1.0 CG F:HIS434 4.1 105.7 1.0 ND1 F:HIS434 4.3 90.2 1.0 OE1 F:GLU435 4.3 110.6 1.0 CG F:HIS438 4.5 113.0 1.0 CD F:GLU435 4.6 100.7 1.0 ND1 F:HIS438 4.7 135.7 1.0 O F:GLY506 4.8 123.8 1.0 CB F:ASP510 4.8 110.5 1.0 OD1 F:ASN509 4.9 167.0 1.0

Zinc binding site 5 out of 6 in the Atp-Dependent Zinc Metalloprotease Ftsh (BB0789) From Borrelia Burgdorferi


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Atp-Dependent Zinc Metalloprotease Ftsh (BB0789) From Borrelia Burgdorferi within 5.0Å range: probe atom residue distance (Å) B Occ I:Zn702 b:80.8 occ:0.00 NE2 I:HIS434 1.9 84.3 1.0 OD2 I:ASP510 2.2 87.9 1.0 NE2 I:HIS438 2.7 91.2 1.0 OD1 I:ASP510 2.7 125.9 1.0 CD2 I:HIS434 2.7 92.4 1.0 CG I:ASP510 2.8 106.9 1.0 CE1 I:HIS434 3.0 99.7 1.0 CD2 I:HIS438 3.4 122.3 1.0 CE1 I:HIS438 3.7 109.1 1.0 CG I:HIS434 3.9 116.5 1.0 ND1 I:HIS434 4.0 108.0 1.0 OE2 I:GLU435 4.2 127.0 1.0 CB I:ASP510 4.3 129.5 1.0 O I:GLY506 4.4 119.1 1.0 CG I:HIS438 4.6 124.5 1.0 ND1 I:HIS438 4.7 112.0 1.0 OD1 I:ASN509 4.7 184.7 1.0 OE1 I:GLU435 4.7 167.3 1.0 CD I:GLU435 4.9 166.6 1.0

Zinc binding site 6 out of 6 in the Atp-Dependent Zinc Metalloprotease Ftsh (BB0789) From Borrelia Burgdorferi


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Atp-Dependent Zinc Metalloprotease Ftsh (BB0789) From Borrelia Burgdorferi within 5.0Å range: probe atom residue distance (Å) B Occ K:Zn702 b:82.7 occ:0.00 NE2 K:HIS434 2.0 71.1 1.0 OD2 K:ASP510 2.6 92.0 1.0 CD2 K:HIS434 2.8 78.3 1.0 OD1 K:ASP510 2.9 120.2 1.0 NE2 K:HIS438 3.0 133.2 1.0 CG K:ASP510 3.1 103.9 1.0 CE1 K:HIS434 3.2 63.2 1.0 CD2 K:HIS438 3.7 146.9 1.0 CG K:HIS434 4.0 89.7 1.0 OE2 K:GLU435 4.0 121.1 1.0 CE1 K:HIS438 4.1 150.3 1.0 ND1 K:HIS434 4.1 74.0 1.0 O K:GLY506 4.3 82.4 1.0 CB K:ASP510 4.6 98.6 1.0 OE1 K:GLU435 4.6 116.8 1.0 CD K:GLU435 4.7 101.7 1.0 CG K:HIS438 4.9 161.6 1.0

K.Brangulis, K.Brangulis. N/A N/A.