Iron in PDB 6fwf: Low Resolution Structure of Neisseria Meningitidis Qnor

All present enzymatic activity of Low Resolution Structure of Neisseria Meningitidis Qnor:
1.7.99.7;

The structure of Low Resolution Structure of Neisseria Meningitidis Qnor, PDB code: 6fwf was solved by D.Young, S.Antonyuk, T.Tosha, T.Hisano, S.Hasnain, Y.Shiro, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	53.64 / 4.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	93.682, 123.096, 130.845, 90.00, 90.00, 90.00
R / Rfree (%)	33.3 / 37.3

The structure of Low Resolution Structure of Neisseria Meningitidis Qnor also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

The binding sites of Iron atom in the Low Resolution Structure of Neisseria Meningitidis Qnor (pdb code 6fwf). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the Low Resolution Structure of Neisseria Meningitidis Qnor, PDB code: 6fwf:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in the Low Resolution Structure of Neisseria Meningitidis Qnor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Low Resolution Structure of Neisseria Meningitidis Qnor within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1001 b:0.7 occ:1.00 FE A:HEM1001 0.0 0.7 1.0 ND A:HEM1001 1.9 0.7 1.0 NE2 A:HIS633 1.9 0.5 1.0 NA A:HEM1001 2.0 0.3 1.0 NB A:HEM1001 2.1 0.1 1.0 NC A:HEM1001 2.1 0.6 1.0 CE1 A:HIS633 2.6 0.4 1.0 C4D A:HEM1001 2.9 0.2 1.0 C1D A:HEM1001 2.9 0.0 1.0 C1A A:HEM1001 3.0 1.0 1.0 CD2 A:HIS633 3.0 0.1 1.0 C4A A:HEM1001 3.1 0.3 1.0 C1B A:HEM1001 3.1 0.3 1.0 C4B A:HEM1001 3.1 0.2 1.0 C4C A:HEM1001 3.1 0.6 1.0 C1C A:HEM1001 3.2 0.3 1.0 FE A:FE1004 3.2 0.9 1.0 CHA A:HEM1001 3.3 0.2 1.0 CHD A:HEM1001 3.4 0.0 1.0 CHB A:HEM1001 3.5 0.6 1.0 CHC A:HEM1001 3.5 0.3 1.0 NE2 A:HIS490 3.6 0.9 1.0 ND1 A:HIS633 3.8 0.5 1.0 CD2 A:HIS490 4.0 0.1 1.0 CG A:HIS633 4.0 0.6 1.0 C3D A:HEM1001 4.1 0.7 1.0 C2D A:HEM1001 4.1 0.9 1.0 C2A A:HEM1001 4.2 0.6 1.0 NE2 A:HIS542 4.2 0.7 1.0 C3A A:HEM1001 4.2 0.3 1.0 C2B A:HEM1001 4.3 0.9 1.0 C3C A:HEM1001 4.3 0.6 1.0 C3B A:HEM1001 4.3 1.0 1.0 C2C A:HEM1001 4.4 0.6 1.0 NE2 A:HIS541 4.4 0.1 1.0 CE1 A:HIS490 4.8 0.1 1.0 CD2 A:HIS542 4.8 0.4 1.0

Iron binding site 2 out of 3 in the Low Resolution Structure of Neisseria Meningitidis Qnor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Low Resolution Structure of Neisseria Meningitidis Qnor within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1002 b:0.8 occ:1.00 FE A:HEM1002 0.0 0.8 1.0 ND A:HEM1002 1.9 0.3 1.0 NE2 A:HIS635 1.9 0.8 1.0 NE2 A:HIS335 2.0 0.2 1.0 NA A:HEM1002 2.0 0.4 1.0 NC A:HEM1002 2.1 0.4 1.0 NB A:HEM1002 2.1 0.2 1.0 CE1 A:HIS635 2.8 0.0 1.0 C4D A:HEM1002 2.9 0.4 1.0 C1D A:HEM1002 2.9 0.7 1.0 CE1 A:HIS335 2.9 0.6 1.0 C1A A:HEM1002 3.0 1.0 1.0 CD2 A:HIS635 3.0 0.6 1.0 CD2 A:HIS335 3.0 0.3 1.0 C4A A:HEM1002 3.1 1.0 1.0 C4C A:HEM1002 3.1 0.9 1.0 C1B A:HEM1002 3.1 0.8 1.0 C4B A:HEM1002 3.1 0.1 1.0 C1C A:HEM1002 3.2 0.5 1.0 CHA A:HEM1002 3.3 0.1 1.0 CHD A:HEM1002 3.4 0.1 1.0 CHB A:HEM1002 3.5 0.6 1.0 CHC A:HEM1002 3.5 0.8 1.0 ND1 A:HIS635 3.9 0.5 1.0 ND1 A:HIS335 4.0 0.1 1.0 CG A:HIS635 4.0 0.5 1.0 C3D A:HEM1002 4.1 0.2 1.0 CG A:HIS335 4.1 0.6 1.0 C2D A:HEM1002 4.1 0.4 1.0 C2A A:HEM1002 4.2 0.3 1.0 C3A A:HEM1002 4.2 0.9 1.0 C3C A:HEM1002 4.3 0.8 1.0 C2B A:HEM1002 4.3 0.7 1.0 C2C A:HEM1002 4.3 0.4 1.0 C3B A:HEM1002 4.4 0.8 1.0 CA A:GLY298 4.7 0.9 1.0

Iron binding site 3 out of 3 in the Low Resolution Structure of Neisseria Meningitidis Qnor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Low Resolution Structure of Neisseria Meningitidis Qnor within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1004 b:0.9 occ:1.00 NE2 A:HIS541 1.9 0.1 1.0 NE2 A:HIS490 1.9 0.9 1.0 NE2 A:HIS542 1.9 0.7 1.0 CD2 A:HIS490 2.3 0.1 1.0 CE1 A:HIS542 2.5 0.6 1.0 CE1 A:HIS490 2.7 0.1 1.0 CD2 A:HIS541 2.8 0.3 1.0 CE1 A:HIS541 2.9 0.6 1.0 CG A:HIS490 3.1 0.6 1.0 CD2 A:HIS542 3.1 0.4 1.0 FE A:HEM1001 3.2 0.7 1.0 ND1 A:HIS490 3.2 0.8 1.0 ND A:HEM1001 3.4 0.7 1.0 NC A:HEM1001 3.6 0.6 1.0 ND1 A:HIS542 3.7 0.7 1.0 C1D A:HEM1001 3.9 0.0 1.0 NA A:HEM1001 3.9 0.3 1.0 CG A:HIS541 4.0 0.7 1.0 CG A:HIS542 4.0 0.7 1.0 ND1 A:HIS541 4.0 0.8 1.0 C4D A:HEM1001 4.0 0.2 1.0 C4C A:HEM1001 4.1 0.6 1.0 NB A:HEM1001 4.2 0.1 1.0 CHD A:HEM1001 4.2 0.0 1.0 CB A:HIS490 4.3 0.6 1.0 C1C A:HEM1001 4.4 0.3 1.0 CHA A:HEM1001 4.5 0.2 1.0 C1A A:HEM1001 4.5 1.0 1.0 C4B A:HEM1001 4.7 0.2 1.0 C2D A:HEM1001 4.7 0.9 1.0 CHC A:HEM1001 4.8 0.3 1.0 C3D A:HEM1001 4.8 0.7 1.0 C4A A:HEM1001 4.9 0.3 1.0 C1B A:HEM1001 5.0 0.3 1.0 O A:THR539 5.0 0.3 1.0

N.Gonska, D.Young, R.Yuki, T.Okamoto, T.Hisano, S.Antonyuk, S.S.Hasnain, K.Muramoto, Y.Shiro, T.Tosha, P.Adelroth. Characterization of the Quinol-Dependent Nitric Oxide Reductase From the Pathogen Neisseria Meningitidis, An Electrogenic Enzyme. Sci Rep V. 8 3637 2018.
ISSN: ESSN 2045-2322
PubMed: 29483528
DOI: 10.1038/S41598-018-21804-0