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Zinc in PDB 2cea: Cell Division Protein Ftsh

Protein crystallography data

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

Other elements in 2cea:

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

Magnesium (Mg) 6 atoms

Zinc Binding Sites:

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 2cea

Go back to Zinc Binding Sites List in 2cea
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 2cea

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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 2cea

Go back to Zinc Binding Sites List in 2cea
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 2cea

Go back to Zinc Binding Sites List in 2cea
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 2cea

Go back to Zinc Binding Sites List in 2cea
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 2cea

Go back to Zinc Binding Sites List in 2cea
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

Reference:

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
Page generated: Wed Dec 16 03:19:14 2020

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