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Iron in PDB 4l2d: X-Ray Structure of the Fe(II) Form of the Iron Superoxide Dismutase From Pseudoalteromonas Haloplanktis

Enzymatic activity of X-Ray Structure of the Fe(II) Form of the Iron Superoxide Dismutase From Pseudoalteromonas Haloplanktis

All present enzymatic activity of X-Ray Structure of the Fe(II) Form of the Iron Superoxide Dismutase From Pseudoalteromonas Haloplanktis:
1.15.1.1;

Protein crystallography data

The structure of X-Ray Structure of the Fe(II) Form of the Iron Superoxide Dismutase From Pseudoalteromonas Haloplanktis, PDB code: 4l2d was solved by I.Russo Krauss, A.Merlino, F.Sica, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.20 / 2.07
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 50.303, 103.625, 89.339, 90.00, 103.68, 90.00
R / Rfree (%) 20 / 22

Iron Binding Sites:

The binding sites of Iron atom in the X-Ray Structure of the Fe(II) Form of the Iron Superoxide Dismutase From Pseudoalteromonas Haloplanktis (pdb code 4l2d). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the X-Ray Structure of the Fe(II) Form of the Iron Superoxide Dismutase From Pseudoalteromonas Haloplanktis, PDB code: 4l2d:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 4l2d

Go back to Iron Binding Sites List in 4l2d
Iron binding site 1 out of 4 in the X-Ray Structure of the Fe(II) Form of the Iron Superoxide Dismutase From Pseudoalteromonas Haloplanktis


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of X-Ray Structure of the Fe(II) Form of the Iron Superoxide Dismutase From Pseudoalteromonas Haloplanktis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe201

b:17.4
occ:1.00
 OD2 A:ASP157 1.9 13.9 1.0
NE2 A:HIS26 2.1 12.7 1.0
NE2 A:HIS73 2.1 16.9 1.0
NE2 A:HIS161 2.1 15.7 1.0
O A:HOH302 2.2 16.3 1.0
CE1 A:HIS26 2.9 13.2 1.0
CD2 A:HIS73 3.0 14.9 1.0
CG A:ASP157 3.0 13.7 1.0
CD2 A:HIS161 3.0 14.9 1.0
CD2 A:HIS26 3.1 13.6 1.0
CE1 A:HIS73 3.1 16.2 1.0
CE1 A:HIS161 3.2 15.2 1.0
OD1 A:ASP157 3.5 14.6 1.0
ND1 A:HIS26 4.0 13.1 1.0
CG A:HIS73 4.1 15.9 1.0
CG A:HIS26 4.2 13.4 1.0
ND1 A:HIS73 4.2 15.9 1.0
CG A:HIS161 4.2 14.7 1.0
ND1 A:HIS161 4.2 14.9 1.0
CB A:ASP157 4.3 13.1 1.0
CB A:TRP159 4.4 12.3 1.0
CH2 A:TRP122 4.4 13.1 1.0
CZ2 A:TRP122 4.6 14.0 1.0
CG A:TRP159 4.7 11.6 1.0
CB A:ALA162 4.9 17.9 1.0

Iron binding site 2 out of 4 in 4l2d

Go back to Iron Binding Sites List in 4l2d
Iron binding site 2 out of 4 in the X-Ray Structure of the Fe(II) Form of the Iron Superoxide Dismutase From Pseudoalteromonas Haloplanktis


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of X-Ray Structure of the Fe(II) Form of the Iron Superoxide Dismutase From Pseudoalteromonas Haloplanktis within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe201

b:15.7
occ:1.00
 OD2 C:ASP157 2.0 14.0 1.0
NE2 C:HIS73 2.1 13.9 1.0
NE2 C:HIS26 2.1 9.5 1.0
NE2 C:HIS161 2.2 14.3 1.0
O C:HOH327 2.3 12.2 1.0
CE1 C:HIS73 3.0 12.9 1.0
CE1 C:HIS26 3.0 11.3 1.0
CG C:ASP157 3.1 14.8 1.0
CD2 C:HIS161 3.1 13.5 1.0
CD2 C:HIS73 3.1 12.8 1.0
CD2 C:HIS26 3.2 11.8 1.0
CE1 C:HIS161 3.3 13.3 1.0
OD1 C:ASP157 3.6 14.3 1.0
ND1 C:HIS73 4.1 12.8 1.0
ND1 C:HIS26 4.2 12.0 1.0
CG C:HIS73 4.2 12.4 1.0
CG C:HIS26 4.3 11.7 1.0
CB C:ASP157 4.3 15.1 1.0
CG C:HIS161 4.3 13.3 1.0
ND1 C:HIS161 4.4 13.6 1.0
CB C:TRP159 4.4 12.8 1.0
CH2 C:TRP122 4.4 14.9 1.0
CZ2 C:TRP122 4.5 14.8 1.0
CG C:TRP159 4.6 12.8 1.0
CB C:ALA162 4.8 15.0 1.0
CD1 C:TRP159 5.0 13.4 1.0

Iron binding site 3 out of 4 in 4l2d

Go back to Iron Binding Sites List in 4l2d
Iron binding site 3 out of 4 in the X-Ray Structure of the Fe(II) Form of the Iron Superoxide Dismutase From Pseudoalteromonas Haloplanktis


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of X-Ray Structure of the Fe(II) Form of the Iron Superoxide Dismutase From Pseudoalteromonas Haloplanktis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe201

b:13.5
occ:1.00
 OD2 B:ASP157 2.0 14.0 1.0
NE2 B:HIS161 2.1 15.2 1.0
NE2 B:HIS73 2.1 16.6 1.0
NE2 B:HIS26 2.2 11.7 1.0
O B:HOH302 2.2 6.5 1.0
CD2 B:HIS73 2.9 16.4 1.0
CG B:ASP157 3.1 14.2 1.0
CE1 B:HIS26 3.1 11.6 1.0
CD2 B:HIS161 3.1 13.3 1.0
CE1 B:HIS161 3.1 15.2 1.0
CE1 B:HIS73 3.2 16.3 1.0
CD2 B:HIS26 3.2 11.6 1.0
OD1 B:ASP157 3.5 13.8 1.0
CG B:HIS73 4.1 15.3 1.0
ND1 B:HIS73 4.2 16.8 1.0
ND1 B:HIS26 4.2 11.8 1.0
ND1 B:HIS161 4.2 15.3 1.0
CG B:HIS161 4.2 14.7 1.0
CG B:HIS26 4.3 12.8 1.0
CB B:ASP157 4.4 15.2 1.0
CH2 B:TRP122 4.4 15.0 1.0
CB B:TRP159 4.4 12.5 1.0
CZ2 B:TRP122 4.6 12.8 1.0
CG B:TRP159 4.7 11.8 1.0
CB B:ALA162 4.9 11.9 1.0

Iron binding site 4 out of 4 in 4l2d

Go back to Iron Binding Sites List in 4l2d
Iron binding site 4 out of 4 in the X-Ray Structure of the Fe(II) Form of the Iron Superoxide Dismutase From Pseudoalteromonas Haloplanktis


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of X-Ray Structure of the Fe(II) Form of the Iron Superoxide Dismutase From Pseudoalteromonas Haloplanktis within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe201

b:14.0
occ:1.00
 OD2 D:ASP157 2.0 13.9 1.0
NE2 D:HIS161 2.2 12.2 1.0
NE2 D:HIS26 2.2 10.2 1.0
NE2 D:HIS73 2.2 14.8 1.0
O D:HOH302 2.4 8.7 1.0
CD2 D:HIS161 3.0 11.9 1.0
CD2 D:HIS73 3.0 14.5 1.0
CE1 D:HIS26 3.1 11.5 1.0
CG D:ASP157 3.1 12.7 1.0
CD2 D:HIS26 3.2 10.3 1.0
CE1 D:HIS73 3.2 14.7 1.0
CE1 D:HIS161 3.3 12.0 1.0
OD1 D:ASP157 3.5 10.2 1.0
ND1 D:HIS26 4.2 11.0 1.0
CG D:HIS161 4.2 12.4 1.0
CG D:HIS73 4.2 13.9 1.0
ND1 D:HIS73 4.3 14.9 1.0
CG D:HIS26 4.3 11.4 1.0
ND1 D:HIS161 4.3 12.4 1.0
CH2 D:TRP122 4.4 12.9 1.0
CB D:ASP157 4.4 13.5 1.0
CB D:TRP159 4.5 10.9 1.0
CZ2 D:TRP122 4.5 12.2 1.0
CB D:ALA162 4.8 12.7 1.0
CG D:TRP159 4.8 11.6 1.0

Reference:

A.Merlino, I.Russo Krauss, I.Castellano, M.R.Ruocco, A.Capasso, E.De Vendittis, B.Rossi, F.Sica. Structural and Denaturation Studies of Two Mutants of A Cold Adapted Superoxide Dismutase Point to the Importance of Electrostatic Interactions in Protein Stability. Biochim.Biophys.Acta V.1844 632 2014.
ISSN: ISSN 0006-3002
PubMed: 24440460
DOI: 10.1016/J.BBAPAP.2014.01.007
Page generated: Mon Aug 5 06:02:54 2024

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