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Magnesium 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:

Zinc (Zn) 6 atoms

Magnesium Binding Sites:

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

Magnesium binding site 1 out of 6 in 2cea

Go back to Magnesium Binding Sites List in 2cea
Magnesium binding site 1 out of 6 in the Cell Division Protein Ftsh


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cell Division Protein Ftsh within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1605

b:47.3
occ:1.00
O A:HOH2046 2.0 33.6 1.0
O2B A:ADP1604 2.2 39.9 1.0
PB A:ADP1604 3.5 32.3 1.0
O2A A:ADP1604 3.7 38.6 1.0
O3B A:ADP1604 3.8 35.5 1.0
O A:HOH2007 3.8 72.6 1.0
O3A A:ADP1604 4.3 34.4 1.0
N A:GLY204 4.4 41.0 1.0
OD1 A:ASP260 4.4 63.4 1.0
O1B A:ADP1604 4.6 39.1 1.0
PA A:ADP1604 4.6 41.4 1.0
NZ A:LYS207 4.7 46.6 1.0
CA A:PRO203 4.7 41.1 1.0
CB A:PRO203 4.7 39.9 1.0
OD2 A:ASP260 4.9 51.0 1.0
OG1 A:THR208 5.0 43.5 1.0

Magnesium binding site 2 out of 6 in 2cea

Go back to Magnesium Binding Sites List in 2cea
Magnesium binding site 2 out of 6 in the Cell Division Protein Ftsh


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Cell Division Protein Ftsh within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1608

b:44.5
occ:1.00
O2B B:ADP1607 2.2 33.3 1.0
O B:HOH2035 2.2 49.3 1.0
PB B:ADP1607 3.4 26.1 1.0
O B:HOH2008 3.5 29.6 1.0
O3B B:ADP1607 3.7 20.3 1.0
NZ B:LYS207 3.9 39.4 1.0
O2A B:ADP1607 4.2 37.4 1.0
OD1 B:ASP260 4.4 52.9 1.0
CA B:PRO203 4.4 40.7 1.0
N B:GLY204 4.4 42.4 1.0
O1B B:ADP1607 4.4 26.4 1.0
OD2 B:ASP260 4.5 59.9 1.0
O3A B:ADP1607 4.5 29.9 1.0
CB B:PRO203 4.6 40.1 1.0
CG B:ASP260 4.9 51.1 1.0
C B:PRO203 5.0 41.0 1.0

Magnesium binding site 3 out of 6 in 2cea

Go back to Magnesium Binding Sites List in 2cea
Magnesium binding site 3 out of 6 in the Cell Division Protein Ftsh


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Cell Division Protein Ftsh within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg1609

b:60.1
occ:1.00
O2B C:ADP1608 2.2 54.2 1.0
PB C:ADP1608 3.2 56.2 1.0
NZ C:LYS207 3.2 45.8 1.0
O3B C:ADP1608 3.4 57.0 1.0
CA C:PRO203 3.4 41.6 1.0
CB C:PRO203 3.7 41.4 1.0
CE C:LYS207 3.8 44.8 1.0
O1B C:ADP1608 3.9 57.9 1.0
N C:GLY204 3.9 41.5 1.0
O2A C:ADP1608 4.1 60.2 1.0
C C:PRO203 4.2 41.3 1.0
N C:PRO203 4.5 40.7 1.0
O3A C:ADP1608 4.5 59.4 1.0
OD1 C:ASN307 4.7 42.3 1.0
OD2 C:ASP260 4.9 44.2 1.0
O C:PRO202 4.9 41.1 1.0
OD1 C:ASP260 5.0 49.3 1.0
CG C:PRO203 5.0 40.6 1.0

Magnesium binding site 4 out of 6 in 2cea

Go back to Magnesium Binding Sites List in 2cea
Magnesium binding site 4 out of 6 in the Cell Division Protein Ftsh


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Cell Division Protein Ftsh within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg1609

b:41.8
occ:1.00
O2A D:ADP1608 2.2 31.8 1.0
O2B D:ADP1608 2.2 30.5 1.0
O D:HOH2006 2.3 58.0 1.0
O D:HOH2033 2.4 38.7 1.0
O D:HOH2032 2.5 50.9 1.0
PB D:ADP1608 2.9 30.1 1.0
O3A D:ADP1608 3.0 26.3 1.0
PA D:ADP1608 3.1 30.5 1.0
O3B D:ADP1608 3.1 21.7 1.0
O D:HOH2034 3.1 31.7 1.0
O5' D:ADP1608 3.5 25.7 1.0
O D:HOH2007 3.7 36.8 1.0
OG1 D:THR208 4.0 34.3 1.0
O1B D:ADP1608 4.3 24.7 1.0
N D:GLY204 4.4 40.9 1.0
O1A D:ADP1608 4.5 24.9 1.0
CA D:GLY204 4.7 41.2 1.0
C5' D:ADP1608 4.7 27.5 1.0
CB D:THR208 4.9 38.7 1.0

Magnesium binding site 5 out of 6 in 2cea

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


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Cell Division Protein Ftsh within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg1605

b:53.2
occ:1.00
O E:HOH2034 2.0 40.6 1.0
O2B E:ADP1604 2.2 43.2 1.0
O2A E:ADP1604 2.2 48.8 1.0
O E:HOH2033 2.2 44.1 1.0
O E:HOH2032 2.3 46.0 1.0
PB E:ADP1604 3.1 42.7 1.0
O3B E:ADP1604 3.1 40.1 1.0
PA E:ADP1604 3.5 38.7 1.0
O3A E:ADP1604 3.6 39.6 1.0
OG1 E:THR208 4.1 48.6 1.0
O5' E:ADP1604 4.1 40.0 1.0
O1B E:ADP1604 4.4 39.1 1.0
N E:GLY204 4.4 41.1 1.0
O1A E:ADP1604 4.7 39.9 1.0
NZ E:LYS207 4.8 43.2 1.0
OD2 E:ASP260 4.9 51.5 1.0
OD1 E:ASP260 4.9 45.7 1.0

Magnesium binding site 6 out of 6 in 2cea

Go back to Magnesium Binding Sites List in 2cea
Magnesium binding site 6 out of 6 in the Cell Division Protein Ftsh


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 6 of Cell Division Protein Ftsh within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mg1608

b:68.0
occ:1.00
O2B F:ADP1607 2.2 73.0 1.0
O2A F:ADP1607 2.6 75.5 1.0
PB F:ADP1607 3.0 77.4 1.0
O3B F:ADP1607 3.1 75.9 1.0
O3A F:ADP1607 3.5 77.8 1.0
PA F:ADP1607 3.6 79.1 1.0
N F:GLY204 4.2 41.7 1.0
O F:HOH2001 4.3 63.1 1.0
O1B F:ADP1607 4.4 72.8 1.0
OD1 F:ASP260 4.6 44.3 1.0
O1A F:ADP1607 4.7 76.2 1.0
O5' F:ADP1607 4.7 79.1 1.0
CA F:PRO203 4.8 41.4 1.0
OG1 F:THR208 4.8 37.1 1.0
CA F:GLY204 4.9 41.6 1.0
C F:PRO203 5.0 41.5 1.0
CB F:PRO203 5.0 40.7 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: Tue Aug 13 22:15:14 2024

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