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

The structure of Crystal Structure of An H-Nox Protein From Nostoc Sp. Pcc 7120, L67W Mutant, PDB code: 3tff 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)	43.56 / 1.94
Space group	P 21 3
Cell size a, b, c (Å), α, β, γ (°)	123.211, 123.211, 123.211, 90.00, 90.00, 90.00
R / Rfree (%)	16.5 / 18.7

The binding sites of Iron atom in the Crystal Structure of An H-Nox Protein From Nostoc Sp. Pcc 7120, L67W Mutant (pdb code 3tff). 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, L67W Mutant, PDB code: 3tff:
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, L67W 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, L67W Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:29.0 occ:1.00 FE A:HEM500 0.0 29.0 1.0 ND A:HEM500 2.0 25.9 1.0 NA A:HEM500 2.1 25.0 1.0 NB A:HEM500 2.1 24.7 1.0 NC A:HEM500 2.1 30.3 1.0 NE2 A:HIS105 2.2 29.4 1.0 HE1 A:TRP74 2.9 38.2 1.0 C4D A:HEM500 3.0 32.3 1.0 C1D A:HEM500 3.1 27.9 1.0 C1A A:HEM500 3.1 25.0 1.0 C4A A:HEM500 3.1 27.4 1.0 C1B A:HEM500 3.1 26.6 1.0 C4C A:HEM500 3.1 29.2 1.0 C4B A:HEM500 3.1 29.2 1.0 CE1 A:HIS105 3.1 33.3 1.0 C1C A:HEM500 3.1 29.1 1.0 CD2 A:HIS105 3.3 27.9 1.0 HE1 A:HIS105 3.3 40.0 1.0 CHA A:HEM500 3.4 28.5 1.0 CHD A:HEM500 3.5 24.4 1.0 CHB A:HEM500 3.5 23.8 1.0 CHC A:HEM500 3.5 33.1 1.0 HD2 A:HIS105 3.5 33.5 1.0 NE1 A:TRP74 3.7 31.8 1.0 HZ2 A:TRP74 4.2 34.4 1.0 C3D A:HEM500 4.3 27.2 1.0 C2D A:HEM500 4.3 25.6 1.0 ND1 A:HIS105 4.3 28.6 1.0 HG3 A:PRO118 4.3 35.2 1.0 C3A A:HEM500 4.3 26.9 1.0 C2A A:HEM500 4.3 27.4 1.0 C3B A:HEM500 4.3 34.9 1.0 C3C A:HEM500 4.3 29.7 1.0 C2B A:HEM500 4.3 30.1 1.0 HD3 A:PRO118 4.4 33.2 1.0 C2C A:HEM500 4.4 30.0 1.0 CG A:HIS105 4.4 25.3 1.0 HD2 A:PRO118 4.4 33.2 1.0 HHB A:HEM500 4.5 28.6 1.0 HHD A:HEM500 4.5 29.2 1.0 HHA A:HEM500 4.5 34.2 1.0 HD11 A:LEU101 4.6 41.2 1.0 CE2 A:TRP74 4.6 29.3 1.0 HHC A:HEM500 4.6 39.7 1.0 CD1 A:TRP74 4.7 34.8 1.0 HD1 A:TRP74 4.7 41.7 1.0 CZ2 A:TRP74 4.8 28.7 1.0 CD A:PRO118 4.8 27.7 1.0 CG A:PRO118 5.0 29.4 1.0 HD22 A:LEU104 5.0 35.1 1.0

Iron binding site 2 out of 2 in the Crystal Structure of An H-Nox Protein From Nostoc Sp. Pcc 7120, L67W 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, L67W Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:26.3 occ:1.00 FE B:HEM501 0.0 26.3 1.0 NA B:HEM501 2.0 25.3 1.0 NC B:HEM501 2.1 26.5 1.0 NB B:HEM501 2.1 29.8 1.0 ND B:HEM501 2.1 27.2 1.0 NE2 B:HIS105 2.2 24.9 1.0 HE1 B:TRP74 3.0 32.1 1.0 CE1 B:HIS105 3.1 33.2 1.0 C1A B:HEM501 3.1 26.3 1.0 C4A B:HEM501 3.1 26.4 1.0 C4B B:HEM501 3.1 26.6 1.0 C4D B:HEM501 3.1 27.8 1.0 C4C B:HEM501 3.1 25.0 1.0 C1B B:HEM501 3.1 29.0 1.0 C1D B:HEM501 3.1 27.9 1.0 C1C B:HEM501 3.1 24.5 1.0 HE1 B:HIS105 3.2 39.8 1.0 CD2 B:HIS105 3.2 25.4 1.0 CHA B:HEM501 3.4 26.5 1.0 CHB B:HEM501 3.5 27.6 1.0 CHD B:HEM501 3.5 21.6 1.0 CHC B:HEM501 3.5 28.1 1.0 HD2 B:HIS105 3.5 30.4 1.0 NE1 B:TRP74 3.8 26.8 1.0 ND1 B:HIS105 4.2 26.4 1.0 C3A B:HEM501 4.3 30.3 1.0 C2A B:HEM501 4.3 27.3 1.0 HZ2 B:TRP74 4.3 32.8 1.0 C3B B:HEM501 4.3 28.0 1.0 HG3 B:PRO118 4.3 30.4 1.0 C3C B:HEM501 4.3 30.0 1.0 C2C B:HEM501 4.3 31.1 1.0 C2B B:HEM501 4.3 28.5 1.0 CG B:HIS105 4.3 26.2 1.0 C2D B:HEM501 4.3 29.4 1.0 C3D B:HEM501 4.4 28.6 1.0 HD2 B:PRO118 4.4 36.0 1.0 HHD B:HEM501 4.5 26.0 1.0 HHB B:HEM501 4.5 33.1 1.0 HHA B:HEM501 4.5 31.8 1.0 HD3 B:PRO118 4.6 36.0 1.0 HD11 B:LEU101 4.6 48.1 1.0 HHC B:HEM501 4.6 33.7 1.0 CE2 B:TRP74 4.7 27.3 1.0 CD1 B:TRP74 4.7 27.2 1.0 HD1 B:TRP74 4.8 32.6 1.0 CD B:PRO118 4.9 30.0 1.0 CZ2 B:TRP74 4.9 27.3 1.0 HD22 B:LEU104 4.9 44.9 1.0 CG B:PRO118 5.0 25.4 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