Iron in PDB 8qta: Cryo-Em Structure of Streptococcus Pneumoniae Nadph Oxidase F397A Mutant in Complex with Nadph

The binding sites of Iron atom in the Cryo-Em Structure of Streptococcus Pneumoniae Nadph Oxidase F397A Mutant in Complex with Nadph (pdb code 8qta). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Cryo-Em Structure of Streptococcus Pneumoniae Nadph Oxidase F397A Mutant in Complex with Nadph, PDB code: 8qta:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Cryo-Em Structure of Streptococcus Pneumoniae Nadph Oxidase F397A Mutant in Complex with Nadph


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cryo-Em Structure of Streptococcus Pneumoniae Nadph Oxidase F397A Mutant in Complex with Nadph within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe503 b:36.5 occ:1.00 FE A:HEM503 0.0 36.5 1.0 ND A:HEM503 1.9 26.6 1.0 NA A:HEM503 2.0 28.7 1.0 NC A:HEM503 2.1 26.3 1.0 NB A:HEM503 2.1 33.6 1.0 NE2 A:HIS83 2.1 33.1 1.0 NE2 A:HIS142 2.2 30.6 1.0 CD2 A:HIS83 2.8 25.7 1.0 C4D A:HEM503 2.9 26.0 1.0 C1D A:HEM503 2.9 29.0 1.0 C1A A:HEM503 2.9 25.9 1.0 C4C A:HEM503 3.0 31.9 1.0 CD2 A:HIS142 3.0 25.5 1.0 C4B A:HEM503 3.1 23.9 1.0 C4A A:HEM503 3.1 30.7 1.0 C1C A:HEM503 3.1 28.1 1.0 C1B A:HEM503 3.1 28.3 1.0 CE1 A:HIS142 3.2 29.1 1.0 CHA A:HEM503 3.3 27.5 1.0 CE1 A:HIS83 3.3 32.0 1.0 CHD A:HEM503 3.4 28.4 1.0 CHC A:HEM503 3.4 25.7 1.0 CHB A:HEM503 3.5 26.5 1.0 CG A:HIS83 4.1 22.2 1.0 C3D A:HEM503 4.1 21.5 1.0 C2D A:HEM503 4.1 25.7 1.0 C2A A:HEM503 4.1 33.0 1.0 C3C A:HEM503 4.2 33.5 1.0 C3A A:HEM503 4.2 35.4 1.0 CG A:HIS142 4.2 22.4 1.0 C2C A:HEM503 4.2 35.8 1.0 ND1 A:HIS142 4.2 29.9 1.0 ND1 A:HIS83 4.3 32.5 1.0 C3B A:HEM503 4.3 23.2 1.0 C2B A:HEM503 4.3 28.9 1.0 CB A:PRO35 5.0 37.2 1.0

Iron binding site 2 out of 2 in the Cryo-Em Structure of Streptococcus Pneumoniae Nadph Oxidase F397A Mutant in Complex with Nadph


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cryo-Em Structure of Streptococcus Pneumoniae Nadph Oxidase F397A Mutant in Complex with Nadph within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe504 b:52.5 occ:1.00 FE A:HEM504 0.0 52.5 1.0 NA A:HEM504 2.1 29.6 1.0 ND A:HEM504 2.1 32.5 1.0 NB A:HEM504 2.1 33.4 1.0 NC A:HEM504 2.1 32.5 1.0 NE2 A:HIS69 2.2 28.7 1.0 NE2 A:HIS129 2.2 13.0 1.0 CE1 A:HIS69 3.0 23.6 1.0 C1A A:HEM504 3.0 27.9 1.0 C4A A:HEM504 3.0 27.8 1.0 C1C A:HEM504 3.1 32.4 1.0 C4B A:HEM504 3.1 28.1 1.0 C1D A:HEM504 3.1 30.3 1.0 C4D A:HEM504 3.1 23.0 1.0 C1B A:HEM504 3.1 25.9 1.0 C4C A:HEM504 3.1 24.5 1.0 CE1 A:HIS129 3.2 23.0 1.0 CD2 A:HIS129 3.2 17.8 1.0 CD2 A:HIS69 3.3 32.6 1.0 CHA A:HEM504 3.4 24.3 1.0 CHC A:HEM504 3.4 30.6 1.0 CHD A:HEM504 3.4 32.8 1.0 CHB A:HEM504 3.4 28.3 1.0 ND1 A:HIS69 4.2 25.4 1.0 C2A A:HEM504 4.2 33.9 1.0 C3A A:HEM504 4.2 26.6 1.0 C2C A:HEM504 4.3 26.6 1.0 C2D A:HEM504 4.3 29.4 1.0 ND1 A:HIS129 4.3 33.0 1.0 C3D A:HEM504 4.3 30.6 1.0 C3B A:HEM504 4.3 31.6 1.0 C2B A:HEM504 4.3 29.0 1.0 C3C A:HEM504 4.3 23.9 1.0 CG A:HIS129 4.3 31.7 1.0 CG A:HIS69 4.3 33.5 1.0 CH2 A:TRP125 5.0 27.0 1.0

V.R.A.Dubach, P.San Seguno-Acosta, B.J.Murphy. Structural and Mechanistic Insights Into Streptococcus Pneumoniae Nadph Oxidase To Be Published 2024.
DOI: 10.1038/S41594-024-01348-W