Iron in PDB 1e14: Photosynthetic Reaction Center Mutant with Phe M197 Replaced with Arg (Chain M, FM197R) and Gly M203 Replaced with Asp (Chain M, GM203D)

The structure of Photosynthetic Reaction Center Mutant with Phe M197 Replaced with Arg (Chain M, FM197R) and Gly M203 Replaced with Asp (Chain M, GM203D), PDB code: 1e14 was solved by P.K.Fyfe, J.P.Ridge, K.E.Mcauley, R.J.Cogdell, N.W.Isaacs, M.R.Jones, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.70
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	140.000, 140.000, 184.600, 90.00, 90.00, 120.00
R / Rfree (%)	22.6 / 26.8

The structure of Photosynthetic Reaction Center Mutant with Phe M197 Replaced with Arg (Chain M, FM197R) and Gly M203 Replaced with Asp (Chain M, GM203D) also contains other interesting chemical elements:

Magnesium

(Mg)

4 atoms

The binding sites of Iron atom in the Photosynthetic Reaction Center Mutant with Phe M197 Replaced with Arg (Chain M, FM197R) and Gly M203 Replaced with Asp (Chain M, GM203D) (pdb code 1e14). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Photosynthetic Reaction Center Mutant with Phe M197 Replaced with Arg (Chain M, FM197R) and Gly M203 Replaced with Asp (Chain M, GM203D), PDB code: 1e14:

Iron binding site 1 out of 1 in the Photosynthetic Reaction Center Mutant with Phe M197 Replaced with Arg (Chain M, FM197R) and Gly M203 Replaced with Asp (Chain M, GM203D)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Photosynthetic Reaction Center Mutant with Phe M197 Replaced with Arg (Chain M, FM197R) and Gly M203 Replaced with Asp (Chain M, GM203D) within 5.0Å range: probe atom residue distance (Å) B Occ M:Fe500 b:31.9 occ:1.00 NE2 L:HIS230 2.1 31.1 1.0 NE2 M:HIS266 2.1 20.3 1.0 NE2 M:HIS219 2.1 33.4 1.0 OE2 M:GLU234 2.1 27.6 1.0 NE2 L:HIS190 2.2 31.3 1.0 OE1 M:GLU234 2.6 27.6 1.0 CD M:GLU234 2.7 28.1 1.0 CE1 M:HIS266 2.9 21.0 1.0 CE1 L:HIS230 3.0 30.6 1.0 CE1 M:HIS219 3.1 34.1 1.0 CE1 L:HIS190 3.1 30.7 1.0 CD2 M:HIS219 3.2 34.4 1.0 CD2 L:HIS230 3.2 32.4 1.0 CD2 L:HIS190 3.2 31.1 1.0 CD2 M:HIS266 3.2 21.5 1.0 ND1 M:HIS266 4.1 20.9 1.0 ND1 L:HIS230 4.2 30.2 1.0 ND1 M:HIS219 4.2 33.8 1.0 CG M:GLU234 4.2 27.0 1.0 ND1 L:HIS190 4.2 30.3 1.0 CG M:HIS266 4.3 22.0 1.0 CG M:HIS219 4.3 33.5 1.0 CG L:HIS230 4.3 31.2 1.0 CG L:HIS190 4.3 30.4 1.0 CG1 M:ILE223 4.4 28.1 1.0 CG2 L:VAL194 4.7 22.2 1.0 O M:HOH2030 4.8 26.7 1.0 CD1 M:ILE223 4.9 29.8 1.0

P.K.Fyfe, J.P.Ridge, K.E.Mcauley, R.J.Cogdell, N.W.Isaacs, M.R.Jones. Structural Consequences of the Replacement of Glycine M203 with Aspartic Acid in the Reaction Center From Rhodobacter Sphaeroides. Biochemistry V. 39 5953 2000.
ISSN: ISSN 0006-2960
PubMed: 10821666
DOI: 10.1021/BI9925017