Iron in PDB 8e7x: Rstspo A138F with One Heme Bound

The structure of Rstspo A138F with One Heme Bound, PDB code: 8e7x was solved by J.Liu, C.Hiser, F.Li, R.Garavito, S.Ferguson-Miller, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.19 / 2.10
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	57.952, 100.103, 95.614, 90, 100.23, 90
R / Rfree (%)	19.6 / 23.2

The binding sites of Iron atom in the Rstspo A138F with One Heme Bound (pdb code 8e7x). 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 Rstspo A138F with One Heme Bound, PDB code: 8e7x:

Iron binding site 1 out of 1 in the Rstspo A138F with One Heme Bound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Rstspo A138F with One Heme Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe202 b:26.2 occ:0.73 FE B:HEM202 0.0 26.2 0.7 NB B:HEM202 2.0 28.6 0.8 NC B:HEM202 2.0 27.5 0.8 NA B:HEM202 2.0 35.7 1.0 ND B:HEM202 2.1 29.5 1.0 O B:HOH308 2.6 27.7 1.0 C4A B:HEM202 3.0 32.9 1.0 C1B B:HEM202 3.0 30.7 1.0 C1D B:HEM202 3.0 30.9 1.0 C4C B:HEM202 3.0 29.0 1.0 C4B B:HEM202 3.1 28.4 0.4 C1A B:HEM202 3.1 33.8 1.0 C1C B:HEM202 3.1 30.7 1.0 C4D B:HEM202 3.1 33.3 1.0 CHB B:HEM202 3.4 31.3 1.0 CHD B:HEM202 3.4 30.4 1.0 CHC B:HEM202 3.4 30.3 1.0 CHA B:HEM202 3.5 34.1 1.0 NE1 B:TRP50 3.9 29.1 1.0 C3A B:HEM202 4.2 31.5 1.0 CD1 B:TRP50 4.3 28.5 1.0 C2D B:HEM202 4.3 31.9 1.0 C2B B:HEM202 4.3 30.5 1.0 C2A B:HEM202 4.3 32.8 1.0 C3B B:HEM202 4.3 29.3 1.0 C3C B:HEM202 4.3 27.6 1.0 C3D B:HEM202 4.3 33.4 1.0 C2C B:HEM202 4.3 26.2 0.6 CD1 B:PHE46 4.3 32.4 1.0 O B:HOH317 4.4 34.7 1.0 CE2 B:PHE92 4.5 28.0 1.0 CZ3 B:TRP87 4.6 26.2 1.0 O B:HOH305 4.6 33.2 1.0 CB B:PHE46 4.7 32.4 1.0 CG B:PHE46 4.7 29.1 1.0 OG1 B:THR88 4.7 22.9 1.0

J.Liu, C.Hiser, F.Li, R.Hall, R.M.Garavito, S.Ferguson-Miller. New Tspo Crystal Structures of Mutant and Heme-Bound Forms with Altered Flexibility, Ligand Binding, and Porphyrin Degradation Activity. Biochemistry 2023.
ISSN: ISSN 0006-2960
PubMed: 36947867
DOI: 10.1021/ACS.BIOCHEM.2C00612