Zinc in PDB 2cea: Cell Division Protein Ftsh

The structure of Cell Division Protein Ftsh, PDB code: 2cea was solved by C.Bieniossek, U.Baumann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 2.75
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	165.316, 165.316, 234.749, 90.00, 90.00, 90.00
R / Rfree (%)	21.6 / 26.2

The structure of Cell Division Protein Ftsh also contains other interesting chemical elements:

Magnesium

(Mg)

6 atoms

The binding sites of Zinc atom in the Cell Division Protein Ftsh (pdb code 2cea). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the Cell Division Protein Ftsh, PDB code: 2cea:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6;

Zinc binding site 1 out of 6 in the Cell Division Protein Ftsh


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Cell Division Protein Ftsh within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1603 b:63.5 occ:1.00 O A:HOH2044 2.0 62.9 1.0 OD2 A:ASP500 2.0 56.5 1.0 NE2 A:HIS423 2.1 57.5 1.0 NE2 A:HIS427 2.1 51.8 1.0 O A:HOH2043 2.3 48.2 1.0 CG A:ASP500 2.9 47.5 1.0 CD2 A:HIS423 2.9 54.2 1.0 CD2 A:HIS427 3.1 48.6 1.0 CE1 A:HIS427 3.1 49.0 1.0 OD1 A:ASP500 3.2 52.0 1.0 CE1 A:HIS423 3.2 54.4 1.0 O A:HOH2014 4.0 63.2 1.0 CG A:HIS423 4.1 48.0 1.0 O A:HOH2027 4.2 25.3 1.0 ND1 A:HIS427 4.2 48.8 1.0 ND1 A:HIS423 4.2 52.9 1.0 CG A:HIS427 4.2 44.3 1.0 CB A:ASP500 4.3 44.4 1.0 OE2 A:GLU424 4.4 67.2 1.0 O A:HOH2023 4.4 53.0 1.0 ND2 A:ASN499 4.7 57.6 1.0 O A:GLY496 5.0 42.8 1.0

Zinc binding site 2 out of 6 in the Cell Division Protein Ftsh


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Cell Division Protein Ftsh within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1606 b:64.2 occ:1.00 O B:HOH2033 2.0 65.7 1.0 OD2 B:ASP500 2.0 60.5 1.0 NE2 B:HIS423 2.1 52.8 1.0 NE2 B:HIS427 2.1 49.7 1.0 CG B:ASP500 2.9 51.8 1.0 CD2 B:HIS423 3.1 49.1 1.0 CD2 B:HIS427 3.1 49.2 1.0 OD1 B:ASP500 3.1 51.3 1.0 CE1 B:HIS427 3.1 47.5 1.0 CE1 B:HIS423 3.1 50.2 1.0 ND1 B:HIS427 4.2 48.6 1.0 ND1 B:HIS423 4.2 46.8 1.0 CG B:HIS423 4.2 45.3 1.0 CG B:HIS427 4.2 47.3 1.0 OE2 B:GLU424 4.3 54.9 1.0 CB B:ASP500 4.3 44.6 1.0 O B:GLY496 4.8 43.8 1.0 ND2 B:ASN499 4.8 63.6 1.0

Zinc binding site 3 out of 6 in the Cell Division Protein Ftsh


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Cell Division Protein Ftsh within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn1607 b:60.6 occ:1.00 O C:HOH2026 2.0 55.1 1.0 OD2 C:ASP500 2.0 49.0 1.0 NE2 C:HIS423 2.1 53.0 1.0 NE2 C:HIS427 2.1 44.5 1.0 CG C:ASP500 2.9 42.8 1.0 CE1 C:HIS423 3.1 51.0 1.0 OD1 C:ASP500 3.1 46.7 1.0 CE1 C:HIS427 3.1 39.4 1.0 CD2 C:HIS423 3.1 45.6 1.0 CD2 C:HIS427 3.2 39.0 1.0 O C:HOH2015 3.8 16.5 1.0 CA C:GLY454 4.1 52.6 1.0 ND1 C:HIS423 4.2 46.6 1.0 ND1 C:HIS427 4.2 40.7 1.0 CG C:HIS423 4.3 44.6 1.0 CG C:HIS427 4.3 40.8 1.0 CB C:ASP500 4.3 41.9 1.0 ND2 C:ASN499 4.4 52.4 1.0 O C:GLY454 4.5 53.5 1.0 C C:GLY454 4.7 54.5 1.0 O C:HOH2007 4.7 62.3 1.0

Zinc binding site 4 out of 6 in the Cell Division Protein Ftsh


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Cell Division Protein Ftsh within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn1607 b:79.3 occ:1.00 OD2 D:ASP500 2.0 61.1 1.0 O D:HOH2031 2.0 72.1 1.0 NE2 D:HIS427 2.1 61.1 1.0 NE2 D:HIS423 2.1 59.3 1.0 CG D:ASP500 2.9 50.6 1.0 CD2 D:HIS423 3.0 54.8 1.0 CD2 D:HIS427 3.0 55.2 1.0 OD1 D:ASP500 3.1 51.4 1.0 CE1 D:HIS427 3.1 56.0 1.0 CE1 D:HIS423 3.2 52.2 1.0 NH1 D:ARG448 4.0 82.5 1.0 OE2 D:GLU424 4.1 57.3 1.0 CG D:HIS427 4.1 50.5 1.0 ND1 D:HIS427 4.1 57.0 1.0 CG D:HIS423 4.2 46.4 1.0 ND1 D:HIS423 4.2 47.8 1.0 CB D:ASP500 4.3 44.5 1.0 CZ D:ARG448 4.4 83.0 1.0 O D:HOH2019 4.4 25.6 1.0 NH2 D:ARG448 4.8 83.9 1.0 NE D:ARG448 4.9 81.5 1.0

Zinc binding site 5 out of 6 in the Cell Division Protein Ftsh


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Cell Division Protein Ftsh within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn1603 b:63.7 occ:1.00 O E:HOH2031 2.0 60.8 1.0 OD2 E:ASP500 2.0 53.9 1.0 NE2 E:HIS423 2.1 51.0 1.0 NE2 E:HIS427 2.1 52.4 1.0 CG E:ASP500 2.7 49.5 1.0 OD1 E:ASP500 2.8 51.4 1.0 CD2 E:HIS423 3.0 49.4 1.0 CD2 E:HIS427 3.1 49.9 1.0 CE1 E:HIS427 3.1 50.3 1.0 CE1 E:HIS423 3.2 52.1 1.0 OE2 E:GLU424 3.9 49.8 1.0 O E:HOH2013 4.0 53.3 1.0 O E:HOH2022 4.2 15.5 1.0 CG E:HIS423 4.2 45.2 1.0 CB E:ASP500 4.2 46.1 1.0 ND1 E:HIS423 4.2 51.0 1.0 ND1 E:HIS427 4.2 44.0 1.0 CG E:HIS427 4.3 45.1 1.0 ND2 E:ASN499 4.5 58.2 1.0

Zinc binding site 6 out of 6 in the Cell Division Protein Ftsh


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Cell Division Protein Ftsh within 5.0Å range: probe atom residue distance (Å) B Occ F:Zn1606 b:69.8 occ:1.00 O F:HOH2024 2.0 53.3 1.0 OD2 F:ASP500 2.0 54.9 1.0 NE2 F:HIS427 2.1 48.3 1.0 NE2 F:HIS423 2.1 52.9 1.0 CG F:ASP500 2.8 48.6 1.0 OD1 F:ASP500 2.9 54.4 1.0 CE1 F:HIS427 3.1 43.4 1.0 CD2 F:HIS423 3.1 49.4 1.0 CD2 F:HIS427 3.1 45.3 1.0 CE1 F:HIS423 3.1 52.2 1.0 O F:HOH2007 3.8 43.6 1.0 ND1 F:HIS427 4.2 42.3 1.0 ND1 F:HIS423 4.2 47.4 1.0 CG F:HIS423 4.2 46.3 1.0 CB F:ASP500 4.2 46.3 1.0 CG F:HIS427 4.2 43.7 1.0 ND2 F:ASN499 4.4 56.9 1.0 O F:HOH2010 4.5 45.1 1.0 O F:LEU479 4.9 41.1 1.0 OD1 F:ASN499 4.9 54.7 1.0 O F:HOH2003 5.0 45.4 1.0

C.Bieniossek, T.Schalch, M.Bumann, M.Meister, R.Meier, U.Baumann. The Molecular Architecture of the Metalloprotease Ftsh. Proc.Natl.Acad.Sci.Usa V. 103 3066 2006.
ISSN: ISSN 0027-8424
PubMed: 16484367
DOI: 10.1073/PNAS.0600031103