Iron in PDB 6cys: Crystal Structure Analysis of the D150G Mutant of Superoxide Dismutase From Trichoderma Reesei

All present enzymatic activity of Crystal Structure Analysis of the D150G Mutant of Superoxide Dismutase From Trichoderma Reesei:
1.15.1.1;

The structure of Crystal Structure Analysis of the D150G Mutant of Superoxide Dismutase From Trichoderma Reesei, PDB code: 6cys was solved by E.Mendoza Rengifo, R.C.Garratt, J.R.S.Ferreira Jr., with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	51.02 / 1.85
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	79.040, 82.010, 133.610, 90.00, 90.00, 90.00
R / Rfree (%)	16 / 19.1

The binding sites of Iron atom in the Crystal Structure Analysis of the D150G Mutant of Superoxide Dismutase From Trichoderma Reesei (pdb code 6cys). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure Analysis of the D150G Mutant of Superoxide Dismutase From Trichoderma Reesei, PDB code: 6cys:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Crystal Structure Analysis of the D150G Mutant of Superoxide Dismutase From Trichoderma Reesei


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure Analysis of the D150G Mutant of Superoxide Dismutase From Trichoderma Reesei within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe301 b:12.1 occ:1.00 OD2 A:ASP163 2.0 12.3 1.0 NE2 A:HIS30 2.1 11.3 1.0 NE2 A:HIS167 2.1 13.6 1.0 NE2 A:HIS78 2.2 13.8 1.0 O A:HOH484 2.2 9.2 1.0 CE1 A:HIS30 3.0 10.6 1.0 CG A:ASP163 3.1 11.9 1.0 CE1 A:HIS167 3.1 12.6 1.0 CE1 A:HIS78 3.1 12.7 1.0 CD2 A:HIS78 3.1 11.7 1.0 HE1 A:HIS30 3.2 12.7 1.0 CD2 A:HIS167 3.2 12.7 1.0 CD2 A:HIS30 3.2 11.3 1.0 HE1 A:HIS167 3.2 15.1 1.0 HE1 A:HIS78 3.3 15.2 1.0 HD2 A:HIS78 3.3 14.0 1.0 HD2 A:HIS167 3.4 15.2 1.0 HD2 A:HIS30 3.4 13.5 1.0 OD1 A:ASP163 3.5 10.5 1.0 HZ2 A:TRP131 3.6 13.7 1.0 HB2 A:TRP165 3.7 12.6 1.0 HE22 A:GLN149 3.8 17.0 1.0 HB2 A:ALA168 4.1 14.9 1.0 ND1 A:HIS30 4.2 12.5 1.0 ND1 A:HIS167 4.2 13.4 1.0 ND1 A:HIS78 4.2 12.8 1.0 CZ2 A:TRP131 4.2 11.4 1.0 CG A:HIS78 4.3 12.2 1.0 CG A:HIS30 4.3 11.6 1.0 CG A:HIS167 4.3 11.5 1.0 CB A:ASP163 4.3 10.0 1.0 HB2 A:ASP163 4.4 12.0 1.0 HE2 A:TYR38 4.4 20.3 1.0 CB A:TRP165 4.5 10.5 1.0 NE2 A:GLN149 4.6 14.2 1.0 HB3 A:ASP163 4.6 12.0 1.0 HB3 A:HIS34 4.6 18.7 1.0 CG A:TRP165 4.7 11.5 1.0 HH2 A:TRP131 4.7 11.6 1.0 HB3 A:TRP165 4.8 12.6 1.0 CH2 A:TRP131 4.8 9.7 1.0 HE21 A:GLN149 4.9 17.0 1.0 CD1 A:TRP165 4.9 12.2 1.0 HE1 A:TRP131 4.9 16.2 1.0 HD1 A:HIS30 4.9 15.0 1.0 HD1 A:HIS167 5.0 16.1 1.0

Iron binding site 2 out of 4 in the Crystal Structure Analysis of the D150G Mutant of Superoxide Dismutase From Trichoderma Reesei


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure Analysis of the D150G Mutant of Superoxide Dismutase From Trichoderma Reesei within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe301 b:10.4 occ:1.00 OD2 B:ASP163 2.0 12.1 1.0 O B:HOH519 2.1 8.4 1.0 NE2 B:HIS78 2.1 11.7 1.0 NE2 B:HIS30 2.2 10.0 1.0 NE2 B:HIS167 2.2 10.0 1.0 CE1 B:HIS78 3.0 10.3 1.0 CG B:ASP163 3.1 9.4 1.0 CE1 B:HIS30 3.1 9.5 1.0 CE1 B:HIS167 3.1 10.4 1.0 CD2 B:HIS30 3.2 10.1 1.0 CD2 B:HIS78 3.2 9.3 1.0 CD2 B:HIS167 3.2 8.9 1.0 HE1 B:HIS78 3.2 12.4 1.0 HE1 B:HIS30 3.3 11.3 1.0 HE1 B:HIS167 3.3 12.5 1.0 HD2 B:HIS30 3.3 12.1 1.0 HD2 B:HIS167 3.3 10.7 1.0 HD2 B:HIS78 3.4 11.2 1.0 OD1 B:ASP163 3.5 8.9 1.0 HZ2 B:TRP131 3.6 10.0 1.0 HB2 B:TRP165 3.7 10.1 1.0 HE22 B:GLN149 3.7 14.1 1.0 HB2 B:ALA168 4.1 12.8 1.0 ND1 B:HIS78 4.2 10.6 1.0 CZ2 B:TRP131 4.2 8.3 1.0 ND1 B:HIS30 4.2 10.1 1.0 ND1 B:HIS167 4.3 10.1 1.0 CG B:HIS78 4.3 9.6 1.0 CG B:HIS30 4.3 10.1 1.0 CB B:ASP163 4.3 8.9 1.0 CG B:HIS167 4.3 8.5 1.0 HB2 B:ASP163 4.4 10.6 1.0 HE2 B:TYR38 4.4 13.7 1.0 CB B:TRP165 4.5 8.4 1.0 HB3 B:ASP163 4.5 10.6 1.0 NE2 B:GLN149 4.6 11.7 1.0 HB3 B:HIS34 4.6 12.1 1.0 CG B:TRP165 4.6 8.6 1.0 HH2 B:TRP131 4.7 10.1 1.0 HB3 B:TRP165 4.8 10.1 1.0 CH2 B:TRP131 4.8 8.4 1.0 HE1 B:TRP131 4.9 12.1 1.0 CD1 B:TRP165 4.9 8.7 1.0 HE21 B:GLN149 4.9 14.1 1.0 HD1 B:HIS78 4.9 12.7 1.0 CE2 B:TRP131 5.0 9.4 1.0 HD1 B:TRP165 5.0 10.4 1.0

Iron binding site 3 out of 4 in the Crystal Structure Analysis of the D150G Mutant of Superoxide Dismutase From Trichoderma Reesei


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure Analysis of the D150G Mutant of Superoxide Dismutase From Trichoderma Reesei within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe301 b:10.4 occ:1.00 OD2 C:ASP163 1.9 11.8 1.0 O C:HOH504 2.1 11.5 1.0 NE2 C:HIS167 2.2 11.1 1.0 NE2 C:HIS78 2.2 11.4 1.0 NE2 C:HIS30 2.2 8.6 1.0 CG C:ASP163 3.1 10.9 1.0 CE1 C:HIS78 3.1 11.1 1.0 CE1 C:HIS167 3.1 9.3 1.0 CE1 C:HIS30 3.2 8.8 1.0 CD2 C:HIS30 3.2 9.1 1.0 CD2 C:HIS167 3.2 9.7 1.0 CD2 C:HIS78 3.2 12.3 1.0 HE1 C:HIS78 3.2 13.3 1.0 HE1 C:HIS167 3.3 11.2 1.0 HD2 C:HIS30 3.3 10.9 1.0 HE1 C:HIS30 3.3 10.5 1.0 HD2 C:HIS167 3.4 11.7 1.0 HD2 C:HIS78 3.4 14.7 1.0 HZ2 C:TRP131 3.5 15.4 1.0 OD1 C:ASP163 3.6 11.6 1.0 HB2 C:TRP165 3.7 11.3 1.0 HE22 C:GLN149 3.7 12.4 1.0 CZ2 C:TRP131 4.1 12.9 1.0 HB2 C:ALA168 4.1 13.1 1.0 ND1 C:HIS78 4.2 11.9 1.0 ND1 C:HIS167 4.2 10.8 1.0 ND1 C:HIS30 4.3 9.3 1.0 CB C:ASP163 4.3 9.8 1.0 CG C:HIS78 4.3 11.6 1.0 CG C:HIS30 4.3 10.0 1.0 CG C:HIS167 4.3 9.6 1.0 HB2 C:ASP163 4.3 11.7 1.0 HE2 C:TYR38 4.4 14.6 1.0 CB C:TRP165 4.5 9.4 1.0 NE2 C:GLN149 4.5 10.4 1.0 HB3 C:ASP163 4.5 11.7 1.0 HH2 C:TRP131 4.6 15.4 1.0 CG C:TRP165 4.6 9.3 1.0 HB3 C:HIS34 4.7 14.4 1.0 CH2 C:TRP131 4.7 12.9 1.0 HB3 C:TRP165 4.7 11.3 1.0 HE21 C:GLN149 4.8 12.4 1.0 CD1 C:TRP165 4.9 9.3 1.0 HE1 C:TRP131 4.9 14.0 1.0 CE2 C:TRP131 4.9 12.0 1.0 HD1 C:TRP165 5.0 11.2 1.0 HD1 C:HIS78 5.0 14.3 1.0

Iron binding site 4 out of 4 in the Crystal Structure Analysis of the D150G Mutant of Superoxide Dismutase From Trichoderma Reesei


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure Analysis of the D150G Mutant of Superoxide Dismutase From Trichoderma Reesei within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe301 b:10.4 occ:1.00 OD2 D:ASP163 2.0 13.3 1.0 O D:HOH511 2.1 9.6 1.0 NE2 D:HIS167 2.1 13.1 1.0 NE2 D:HIS78 2.2 12.8 1.0 NE2 D:HIS30 2.2 9.6 1.0 CE1 D:HIS78 3.0 14.0 1.0 CG D:ASP163 3.1 10.0 1.0 CE1 D:HIS167 3.1 11.8 1.0 CE1 D:HIS30 3.1 9.5 1.0 HE1 D:HIS78 3.2 16.8 1.0 CD2 D:HIS167 3.2 11.8 1.0 CD2 D:HIS78 3.2 13.1 1.0 HE1 D:HIS30 3.2 11.4 1.0 CD2 D:HIS30 3.2 9.3 1.0 HE1 D:HIS167 3.2 14.1 1.0 HD2 D:HIS167 3.4 14.1 1.0 HD2 D:HIS78 3.4 15.7 1.0 HD2 D:HIS30 3.4 11.1 1.0 OD1 D:ASP163 3.5 11.8 1.0 HZ2 D:TRP131 3.5 11.3 1.0 HB2 D:TRP165 3.6 11.9 1.0 HE22 D:GLN149 3.7 11.5 1.0 HB2 D:ALA168 4.1 11.9 1.0 CZ2 D:TRP131 4.1 9.5 1.0 ND1 D:HIS78 4.2 13.1 1.0 ND1 D:HIS167 4.2 12.7 1.0 ND1 D:HIS30 4.2 10.7 1.0 CG D:HIS78 4.3 11.9 1.0 CG D:HIS167 4.3 11.5 1.0 CG D:HIS30 4.3 8.7 1.0 CB D:ASP163 4.3 8.9 1.0 HB2 D:ASP163 4.4 10.6 1.0 CB D:TRP165 4.5 10.0 1.0 NE2 D:GLN149 4.5 9.6 1.0 HE2 D:TYR38 4.5 17.3 1.0 HH2 D:TRP131 4.6 11.2 1.0 HB3 D:ASP163 4.6 10.6 1.0 CG D:TRP165 4.6 9.2 1.0 HB3 D:HIS34 4.6 15.5 1.0 CH2 D:TRP131 4.7 9.3 1.0 HB3 D:TRP165 4.7 11.9 1.0 HE21 D:GLN149 4.9 11.5 1.0 HE1 D:TRP131 4.9 13.1 1.0 CE2 D:TRP131 4.9 10.1 1.0 CD1 D:TRP165 4.9 10.4 1.0 HD1 D:HIS78 4.9 15.7 1.0 HD1 D:HIS167 5.0 15.2 1.0 HD1 D:HIS30 5.0 12.8 1.0

E.Mendoza Rengifo, R.C.Garratt, J.R.S.Ferreira Jr.. Crystal Structure Analysis of the D150G Mutant of Superoxide Dismutase From Trichoderma Reesei To Be Published.