Iron in PDB 3tfg: Crystal Structure of An H-Nox Protein From Nostoc Sp. Pcc 7120, L66W/L67W Double Mutant

The structure of Crystal Structure of An H-Nox Protein From Nostoc Sp. Pcc 7120, L66W/L67W Double Mutant, PDB code: 3tfg was solved by M.B.Winter, M.A.Herzik Jr., J.Kuriyan, M.A.Marletta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.53 / 1.90
Space group	P 21 3
Cell size a, b, c (Å), α, β, γ (°)	123.123, 123.123, 123.123, 90.00, 90.00, 90.00
R / Rfree (%)	16 / 18.3

The binding sites of Iron atom in the Crystal Structure of An H-Nox Protein From Nostoc Sp. Pcc 7120, L66W/L67W Double Mutant (pdb code 3tfg). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of An H-Nox Protein From Nostoc Sp. Pcc 7120, L66W/L67W Double Mutant, PDB code: 3tfg:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of An H-Nox Protein From Nostoc Sp. Pcc 7120, L66W/L67W Double Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of An H-Nox Protein From Nostoc Sp. Pcc 7120, L66W/L67W Double Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:23.1 occ:1.00 FE A:HEM500 0.0 23.1 1.0 ND A:HEM500 2.0 22.8 1.0 NB A:HEM500 2.1 21.2 1.0 NA A:HEM500 2.1 19.9 1.0 NC A:HEM500 2.1 25.5 1.0 NE2 A:HIS105 2.2 23.1 1.0 HE1 A:TRP74 3.0 24.5 1.0 C1A A:HEM500 3.0 19.3 1.0 C4D A:HEM500 3.1 21.3 1.0 C4C A:HEM500 3.1 22.6 1.0 C1D A:HEM500 3.1 23.9 1.0 C4B A:HEM500 3.1 22.4 1.0 C4A A:HEM500 3.1 20.3 1.0 C1C A:HEM500 3.1 22.6 1.0 C1B A:HEM500 3.1 23.6 1.0 CE1 A:HIS105 3.2 25.1 1.0 CD2 A:HIS105 3.2 22.9 1.0 HE1 A:HIS105 3.3 24.5 1.0 HD2 A:HIS105 3.4 21.9 1.0 CHD A:HEM500 3.4 20.4 1.0 CHA A:HEM500 3.4 20.5 1.0 CHC A:HEM500 3.5 25.0 1.0 CHB A:HEM500 3.5 18.9 1.0 NE1 A:TRP74 3.8 25.0 1.0 C3D A:HEM500 4.3 19.6 1.0 C2A A:HEM500 4.3 19.5 1.0 C3C A:HEM500 4.3 26.6 1.0 C2D A:HEM500 4.3 26.0 1.0 ND1 A:HIS105 4.3 22.8 1.0 C3A A:HEM500 4.3 20.7 1.0 HZ2 A:TRP74 4.3 24.4 1.0 C3B A:HEM500 4.3 25.6 1.0 HHB A:HEM500 4.3 18.9 1.0 HHD A:HEM500 4.4 20.4 1.0 CG A:HIS105 4.4 21.7 1.0 C2B A:HEM500 4.4 25.5 1.0 C2C A:HEM500 4.4 25.0 1.0 HD3 A:PRO118 4.4 21.3 1.0 HHA A:HEM500 4.4 20.5 1.0 HHC A:HEM500 4.4 25.0 1.0 HG3 A:PRO118 4.4 21.4 1.0 HD2 A:PRO118 4.5 21.3 1.0 CE2 A:TRP74 4.6 25.9 1.0 CD1 A:TRP74 4.7 25.7 1.0 HD11 A:LEU101 4.7 30.3 1.0 HD1 A:TRP74 4.8 25.2 1.0 CD A:PRO118 4.8 24.3 1.0 CZ2 A:TRP74 4.8 25.0 1.0 HD22 A:LEU104 4.9 27.0 1.0 CG A:PRO118 5.0 24.0 1.0

Iron binding site 2 out of 2 in the Crystal Structure of An H-Nox Protein From Nostoc Sp. Pcc 7120, L66W/L67W Double Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of An H-Nox Protein From Nostoc Sp. Pcc 7120, L66W/L67W Double Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:22.2 occ:1.00 FE B:HEM501 0.0 22.2 1.0 NA B:HEM501 2.0 19.8 1.0 NC B:HEM501 2.1 25.0 1.0 NB B:HEM501 2.1 21.6 1.0 ND B:HEM501 2.1 22.8 1.0 NE2 B:HIS105 2.2 21.9 1.0 HE1 B:TRP74 3.0 18.8 1.0 C1B B:HEM501 3.1 19.8 1.0 C1C B:HEM501 3.1 21.7 1.0 C4C B:HEM501 3.1 19.7 1.0 C1A B:HEM501 3.1 19.1 1.0 C4A B:HEM501 3.1 18.8 1.0 C1D B:HEM501 3.1 22.2 1.0 C4B B:HEM501 3.1 20.8 1.0 C4D B:HEM501 3.1 23.4 1.0 CE1 B:HIS105 3.2 25.6 1.0 CD2 B:HIS105 3.2 22.6 1.0 HE1 B:HIS105 3.3 23.5 1.0 HD2 B:HIS105 3.4 20.7 1.0 CHB B:HEM501 3.5 21.3 1.0 CHD B:HEM501 3.5 21.4 1.0 CHA B:HEM501 3.5 20.6 1.0 CHC B:HEM501 3.5 20.8 1.0 NE1 B:TRP74 3.8 20.3 1.0 HZ2 B:TRP74 4.2 21.3 1.0 C2C B:HEM501 4.3 22.4 1.0 HHD B:HEM501 4.3 21.4 1.0 C3C B:HEM501 4.3 22.8 1.0 ND1 B:HIS105 4.3 25.3 1.0 C3A B:HEM501 4.3 23.0 1.0 C3B B:HEM501 4.3 22.2 1.0 C2A B:HEM501 4.3 23.6 1.0 C2B B:HEM501 4.3 20.7 1.0 C2D B:HEM501 4.3 20.4 1.0 C3D B:HEM501 4.3 22.5 1.0 CG B:HIS105 4.4 19.7 1.0 HG3 B:PRO118 4.4 21.8 1.0 HHB B:HEM501 4.4 21.3 1.0 HHC B:HEM501 4.4 20.8 1.0 HHA B:HEM501 4.4 20.6 1.0 HD2 B:PRO118 4.5 23.3 1.0 HD3 B:PRO118 4.5 23.3 1.0 CE2 B:TRP74 4.6 20.7 1.0 HD11 B:LEU101 4.7 44.5 1.0 CD1 B:TRP74 4.7 22.0 1.0 CZ2 B:TRP74 4.7 22.3 1.0 HD1 B:TRP74 4.8 20.6 1.0 CD B:PRO118 4.8 24.0 1.0 HD22 B:LEU104 4.9 31.1 1.0 CG B:PRO118 5.0 22.4 1.0

M.B.Winter, M.A.Herzik, J.Kuriyan, M.A.Marletta. Tunnels Modulate Ligand Flux in A Heme Nitric Oxide/Oxygen Binding (H-Nox) Domain. Proc.Natl.Acad.Sci.Usa V. 108 E881 2011.
ISSN: ISSN 0027-8424
PubMed: 21997213
DOI: 10.1073/PNAS.1114038108