Iron in PDB 4m1i: X-Ray Crystal Structure of Chlamydia Trachomatis Mn(II)Fe(II)-Nrdb

All present enzymatic activity of X-Ray Crystal Structure of Chlamydia Trachomatis Mn(II)Fe(II)-Nrdb:
1.17.4.1;

The structure of X-Ray Crystal Structure of Chlamydia Trachomatis Mn(II)Fe(II)-Nrdb, PDB code: 4m1i was solved by A.K.Boal, A.C.Rosenzweig, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.85 / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	74.897, 97.455, 99.315, 90.00, 97.77, 90.00
R / Rfree (%)	17.2 / 20.2

The structure of X-Ray Crystal Structure of Chlamydia Trachomatis Mn(II)Fe(II)-Nrdb also contains other interesting chemical elements:

Manganese

(Mn)

4 atoms

The binding sites of Iron atom in the X-Ray Crystal Structure of Chlamydia Trachomatis Mn(II)Fe(II)-Nrdb (pdb code 4m1i). 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 Crystal Structure of Chlamydia Trachomatis Mn(II)Fe(II)-Nrdb, PDB code: 4m1i:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the X-Ray Crystal Structure of Chlamydia Trachomatis Mn(II)Fe(II)-Nrdb


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of X-Ray Crystal Structure of Chlamydia Trachomatis Mn(II)Fe(II)-Nrdb within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe402 b:16.4 occ:1.00 OE2 A:GLU193 1.9 15.6 1.0 OE2 A:GLU227 2.1 17.2 1.0 O A:HOH501 2.1 17.9 1.0 OE2 A:GLU120 2.1 13.5 1.0 OE1 A:GLU227 2.2 16.1 1.0 ND1 A:HIS230 2.2 9.9 1.0 CD A:GLU227 2.4 19.3 1.0 CE1 A:HIS230 3.0 10.0 1.0 CD A:GLU193 3.0 15.4 1.0 CD A:GLU120 3.0 13.1 1.0 MN A:MN401 3.2 14.4 0.9 OE1 A:GLU120 3.2 13.9 1.0 CG A:HIS230 3.3 9.9 1.0 CG A:GLU193 3.4 13.5 1.0 CB A:HIS230 3.8 9.3 1.0 CG A:GLU227 3.9 16.2 1.0 OE1 A:GLU193 4.1 17.6 1.0 OE1 A:GLN116 4.1 14.4 1.0 NE2 A:HIS230 4.2 8.5 1.0 CG1 A:VAL92 4.2 7.9 1.0 CD2 A:HIS230 4.3 9.3 1.0 CB A:GLU193 4.4 12.2 1.0 O A:HOH502 4.4 13.5 1.0 CG A:GLU120 4.4 10.2 1.0 CE2 A:PHE197 4.6 17.2 1.0 CB A:GLU227 4.7 12.7 1.0 CA A:GLU227 4.8 11.9 1.0 ND1 A:HIS123 4.8 10.2 1.0 CE1 A:HIS123 4.8 10.5 1.0 CD2 A:PHE197 4.9 16.6 1.0 CG A:GLN116 4.9 8.7 1.0 OE1 A:GLU89 4.9 14.7 1.0 CD A:GLN116 4.9 11.1 1.0

Iron binding site 2 out of 4 in the X-Ray Crystal Structure of Chlamydia Trachomatis Mn(II)Fe(II)-Nrdb


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of X-Ray Crystal Structure of Chlamydia Trachomatis Mn(II)Fe(II)-Nrdb within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe401 b:17.9 occ:1.00 OE2 B:GLU193 2.0 14.9 1.0 OE2 B:GLU120 2.1 14.6 1.0 O B:HOH501 2.1 12.3 1.0 OE2 B:GLU227 2.1 16.4 1.0 ND1 B:HIS230 2.2 11.3 1.0 OE1 B:GLU227 2.2 15.2 1.0 CD B:GLU227 2.5 17.8 1.0 CD B:GLU120 3.0 15.0 1.0 CE1 B:HIS230 3.0 9.8 1.0 CD B:GLU193 3.1 14.6 1.0 OE1 B:GLU120 3.2 16.7 1.0 MN B:MN402 3.2 15.3 0.8 CG B:HIS230 3.3 10.3 1.0 CG B:GLU193 3.5 13.3 1.0 CB B:HIS230 3.8 10.3 1.0 CG B:GLU227 4.0 14.4 1.0 CG1 B:VAL92 4.0 10.4 1.0 OE1 B:GLN116 4.1 14.5 1.0 OE1 B:GLU193 4.1 16.4 1.0 NE2 B:HIS230 4.2 8.6 1.0 CD2 B:HIS230 4.4 9.5 1.0 CG B:GLU120 4.4 10.9 1.0 CB B:GLU193 4.4 12.5 1.0 O B:HOH502 4.5 17.9 1.0 CE2 B:PHE197 4.5 18.9 1.0 CA B:GLU227 4.8 12.9 1.0 CG B:GLN116 4.8 8.4 1.0 CB B:GLU227 4.8 12.8 1.0 CE1 B:HIS123 4.9 10.5 1.0 OE1 B:GLU89 4.9 18.8 1.0 ND1 B:HIS123 4.9 11.6 1.0 CD B:GLN116 4.9 10.3 1.0 CB B:VAL92 4.9 11.1 1.0

Iron binding site 3 out of 4 in the X-Ray Crystal Structure of Chlamydia Trachomatis Mn(II)Fe(II)-Nrdb


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of X-Ray Crystal Structure of Chlamydia Trachomatis Mn(II)Fe(II)-Nrdb within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe401 b:18.0 occ:1.00 OE2 C:GLU193 1.9 17.1 1.0 OE2 C:GLU227 2.1 18.2 1.0 O C:HOH501 2.1 18.4 1.0 OE1 C:GLU227 2.1 17.9 1.0 OE2 C:GLU120 2.1 15.5 1.0 ND1 C:HIS230 2.2 12.7 1.0 CD C:GLU227 2.4 20.1 1.0 CD C:GLU193 3.0 17.6 1.0 CE1 C:HIS230 3.0 12.6 1.0 CD C:GLU120 3.0 17.1 1.0 MN C:MN402 3.2 16.6 0.8 OE1 C:GLU120 3.2 19.0 1.0 CG C:HIS230 3.3 12.0 1.0 CG C:GLU193 3.4 17.1 1.0 CB C:HIS230 3.7 12.2 1.0 CG C:GLU227 3.9 17.1 1.0 OE1 C:GLU193 4.0 18.4 1.0 OE1 C:GLN116 4.1 15.1 1.0 NE2 C:HIS230 4.2 11.3 1.0 CG1 C:VAL92 4.3 13.6 1.0 CD2 C:HIS230 4.3 11.1 1.0 O C:HOH502 4.3 16.6 1.0 CB C:GLU193 4.4 16.2 1.0 CG C:GLU120 4.4 14.2 1.0 CE2 C:PHE197 4.7 22.2 1.0 CB C:GLU227 4.7 14.3 1.0 CA C:GLU227 4.8 14.0 1.0 CE1 C:HIS123 4.8 13.3 1.0 ND1 C:HIS123 4.8 13.1 1.0 OE1 C:GLU89 4.8 21.5 1.0 CG C:GLN116 4.9 11.2 1.0 CD2 C:PHE197 4.9 21.2 1.0 CD C:GLN116 5.0 12.7 1.0

Iron binding site 4 out of 4 in the X-Ray Crystal Structure of Chlamydia Trachomatis Mn(II)Fe(II)-Nrdb


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of X-Ray Crystal Structure of Chlamydia Trachomatis Mn(II)Fe(II)-Nrdb within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe401 b:19.3 occ:1.00 OE2 D:GLU193 1.9 19.4 1.0 O D:HOH501 2.1 17.3 1.0 OE2 D:GLU120 2.1 15.6 1.0 OE1 D:GLU227 2.1 19.0 1.0 ND1 D:HIS230 2.2 12.3 1.0 OE2 D:GLU227 2.2 18.9 1.0 CD D:GLU227 2.5 21.1 1.0 CD D:GLU193 3.0 19.3 1.0 CE1 D:HIS230 3.0 12.5 1.0 CD D:GLU120 3.0 16.0 1.0 MN D:MN402 3.2 15.9 0.8 OE1 D:GLU120 3.2 18.0 1.0 CG D:HIS230 3.3 12.2 1.0 CG D:GLU193 3.5 17.7 1.0 CB D:HIS230 3.8 12.8 1.0 CG D:GLU227 4.0 17.0 1.0 OE1 D:GLU193 4.0 21.0 1.0 OE1 D:GLN116 4.1 15.8 1.0 NE2 D:HIS230 4.2 11.3 1.0 CG1 D:VAL92 4.2 13.7 1.0 CD2 D:HIS230 4.3 11.7 1.0 CG D:GLU120 4.4 13.3 1.0 O D:HOH502 4.4 20.8 1.0 CB D:GLU193 4.4 16.2 1.0 CE2 D:PHE197 4.6 19.2 1.0 CE1 D:HIS123 4.7 13.0 1.0 ND1 D:HIS123 4.8 12.2 1.0 CA D:GLU227 4.8 14.6 1.0 CB D:GLU227 4.8 15.4 1.0 OE1 D:GLU89 4.8 19.9 1.0 CG D:GLN116 4.9 11.8 1.0 CD D:GLN116 4.9 13.4 1.0

L.M.Dassama, C.Krebs, J.M.Bollinger, A.C.Rosenzweig, A.K.Boal. Structural Basis For Assembly of the Mn(IV)/Fe(III) Cofactor in the Class Ic Ribonucleotide Reductase From Chlamydia Trachomatis. Biochemistry V. 52 6424 2013.
ISSN: ISSN 0006-2960
PubMed: 23924396
DOI: 10.1021/BI400819X