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Iron in PDB 1mps: Photosynthetic Reaction Center Mutant with Phe M 197 Replaced with Arg and Tyr M 177 Replaced with Phe (Chain M, Y177F, F197R)

Protein crystallography data

The structure of Photosynthetic Reaction Center Mutant with Phe M 197 Replaced with Arg and Tyr M 177 Replaced with Phe (Chain M, Y177F, F197R), PDB code: 1mps was solved by K.E.Mcauley-Hecht, P.K.Fyfe, J.P.Ridge, S.Prince, C.N.Hunter, N.W.Isaacs, R.J.Cogdell, M.R.Jones, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 11.00 / 2.55
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 141.900, 141.900, 187.900, 90.00, 90.00, 120.00
R / Rfree (%) 19.4 / 21.7

Other elements in 1mps:

The structure of Photosynthetic Reaction Center Mutant with Phe M 197 Replaced with Arg and Tyr M 177 Replaced with Phe (Chain M, Y177F, F197R) also contains other interesting chemical elements:

Magnesium (Mg) 4 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Photosynthetic Reaction Center Mutant with Phe M 197 Replaced with Arg and Tyr M 177 Replaced with Phe (Chain M, Y177F, F197R) (pdb code 1mps). 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 M 197 Replaced with Arg and Tyr M 177 Replaced with Phe (Chain M, Y177F, F197R), PDB code: 1mps:

Iron binding site 1 out of 1 in 1mps

Go back to Iron Binding Sites List in 1mps
Iron binding site 1 out of 1 in the Photosynthetic Reaction Center Mutant with Phe M 197 Replaced with Arg and Tyr M 177 Replaced with Phe (Chain M, Y177F, F197R)


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 M 197 Replaced with Arg and Tyr M 177 Replaced with Phe (Chain M, Y177F, F197R) within 5.0Å range:
probe atom residue distance (Å) B Occ
M:Fe500

b:23.6
occ:1.00
NE2 M:HIS219 2.2 34.9 1.0
NE2 L:HIS190 2.2 15.3 1.0
NE2 M:HIS266 2.2 24.8 1.0
OE2 M:GLU234 2.2 27.5 1.0
NE2 L:HIS230 2.2 22.6 1.0
OE1 M:GLU234 2.2 27.4 1.0
CD M:GLU234 2.5 24.6 1.0
CE1 M:HIS219 3.1 30.6 1.0
CD2 L:HIS190 3.1 20.2 1.0
CD2 M:HIS266 3.2 21.3 1.0
CD2 L:HIS230 3.2 27.1 1.0
CE1 L:HIS190 3.2 40.7 1.0
CE1 M:HIS266 3.2 27.1 1.0
CD2 M:HIS219 3.2 33.1 1.0
CE1 L:HIS230 3.2 27.8 1.0
CG M:GLU234 4.0 26.7 1.0
ND1 M:HIS219 4.3 34.8 1.0
CG L:HIS190 4.3 30.6 1.0
ND1 L:HIS190 4.3 41.1 1.0
CG M:HIS219 4.4 32.3 1.0
CG M:HIS266 4.4 23.0 1.0
ND1 M:HIS266 4.4 27.7 1.0
ND1 L:HIS230 4.4 38.2 1.0
CG L:HIS230 4.4 27.6 1.0
CG1 M:ILE223 4.7 6.0 1.0
CG2 L:VAL194 4.7 20.3 1.0
CB M:GLU234 5.0 20.1 1.0

Reference:

K.E.Mcauley-Hecht, P.K.Fyfe, J.P.Ridge, S.M.Prince, C.N.Hunter, N.W.Isaacs, R.J.Cogdell, M.R.Jones. Structural Studies of Wild-Type and Mutant Reaction Centers From An Antenna-Deficient Strain of Rhodobacter Sphaeroides: Monitoring the Optical Properties of the Complex From Bacterial Cell to Crystal. Biochemistry V. 37 4740 1998.
ISSN: ISSN 0006-2960
PubMed: 9537989
DOI: 10.1021/BI971717A
Page generated: Wed Jul 16 18:17:03 2025

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