Iron in PDB 3tf0: Crystal Structure of An H-Nox Protein From T. Tengcongensis

The structure of Crystal Structure of An H-Nox Protein From T. Tengcongensis, PDB code: 3tf0 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)	38.47 / 1.74
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	80.502, 130.766, 42.736, 90.00, 90.00, 90.00
R / Rfree (%)	20.2 / 22.9

The binding sites of Iron atom in the Crystal Structure of An H-Nox Protein From T. Tengcongensis (pdb code 3tf0). 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 T. Tengcongensis, PDB code: 3tf0:
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 T. Tengcongensis


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 T. Tengcongensis within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:19.3 occ:1.00 FE A:HEM500 0.0 19.3 1.0 O1 A:OXY501 1.9 20.6 1.0 NA A:HEM500 2.0 15.4 1.0 NC A:HEM500 2.0 19.6 1.0 NB A:HEM500 2.0 18.4 1.0 ND A:HEM500 2.1 18.5 1.0 NE2 A:HIS102 2.1 22.9 1.0 O2 A:OXY501 2.8 21.9 1.0 C4A A:HEM500 3.0 17.8 1.0 CE1 A:HIS102 3.0 20.6 1.0 C4C A:HEM500 3.0 14.5 1.0 C1D A:HEM500 3.0 17.8 1.0 C1B A:HEM500 3.0 20.5 1.0 C1A A:HEM500 3.0 17.8 1.0 C4B A:HEM500 3.0 17.9 1.0 C4D A:HEM500 3.1 19.3 1.0 C1C A:HEM500 3.1 16.9 1.0 CD2 A:HIS102 3.1 19.2 1.0 HE1 A:HIS102 3.2 24.8 1.0 CHD A:HEM500 3.4 18.3 1.0 CHB A:HEM500 3.4 17.4 1.0 HD2 A:HIS102 3.4 23.0 1.0 CHA A:HEM500 3.4 18.0 1.0 CHC A:HEM500 3.4 17.3 1.0 HE2 A:PHE78 3.8 17.4 1.0 HD13 A:LEU144 3.8 24.9 1.0 HZ A:PHE78 4.1 23.3 1.0 ND1 A:HIS102 4.2 19.4 1.0 HE2 A:TYR140 4.2 23.7 1.0 C3A A:HEM500 4.2 23.1 1.0 C2D A:HEM500 4.2 17.6 1.0 C2A A:HEM500 4.2 20.4 1.0 CG A:HIS102 4.2 16.9 1.0 C3C A:HEM500 4.2 13.6 1.0 C3D A:HEM500 4.2 19.0 1.0 C2B A:HEM500 4.3 23.3 1.0 C3B A:HEM500 4.3 20.0 1.0 C2C A:HEM500 4.3 15.5 1.0 HH A:TYR140 4.3 22.5 1.0 HD11 A:LEU144 4.3 24.9 1.0 HD11 A:LEU117 4.4 29.1 1.0 HHD A:HEM500 4.4 22.0 1.0 HHB A:HEM500 4.5 20.9 1.0 HHA A:HEM500 4.5 21.6 1.0 HHC A:HEM500 4.5 20.8 1.0 CE2 A:PHE78 4.5 14.5 1.0 CD1 A:LEU144 4.6 20.8 1.0 CZ A:PHE78 4.7 19.4 1.0 HG3 A:PRO115 4.7 23.7 1.0 HD12 A:ILE5 4.9 30.1 1.0 HG21 A:ILE5 5.0 35.5 1.0 HG2 A:PRO115 5.0 23.7 1.0

Iron binding site 2 out of 2 in the Crystal Structure of An H-Nox Protein From T. Tengcongensis


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 T. Tengcongensis within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe503 b:20.9 occ:1.00 FE B:HEM503 0.0 20.9 1.0 O1 B:OXY504 2.0 23.4 1.0 NA B:HEM503 2.0 17.7 1.0 NC B:HEM503 2.0 17.4 1.0 NB B:HEM503 2.0 17.2 1.0 ND B:HEM503 2.0 20.1 1.0 NE2 B:HIS102 2.1 25.3 1.0 O2 B:OXY504 2.8 22.7 1.0 CE1 B:HIS102 3.0 24.4 1.0 C4A B:HEM503 3.0 16.5 1.0 C1D B:HEM503 3.0 18.2 1.0 C4C B:HEM503 3.0 16.6 1.0 C1B B:HEM503 3.0 16.8 1.0 C1A B:HEM503 3.0 19.2 1.0 C4D B:HEM503 3.0 20.6 1.0 C4B B:HEM503 3.1 15.8 1.0 C1C B:HEM503 3.1 20.1 1.0 HE1 B:HIS102 3.1 29.3 1.0 CD2 B:HIS102 3.2 23.6 1.0 CHB B:HEM503 3.3 17.4 1.0 CHD B:HEM503 3.3 18.6 1.0 CHA B:HEM503 3.4 24.4 1.0 HD2 B:HIS102 3.5 28.3 1.0 CHC B:HEM503 3.5 20.1 1.0 HE2 B:PHE78 3.9 21.6 1.0 HD13 B:LEU144 3.9 23.1 1.0 HZ B:PHE78 4.1 26.4 1.0 ND1 B:HIS102 4.1 25.4 1.0 C3A B:HEM503 4.2 24.2 1.0 C2D B:HEM503 4.2 20.7 1.0 HE2 B:TYR140 4.2 23.6 1.0 C2A B:HEM503 4.2 19.4 1.0 C2B B:HEM503 4.2 18.7 1.0 C3D B:HEM503 4.2 19.6 1.0 C3C B:HEM503 4.2 15.6 1.0 CG B:HIS102 4.3 22.2 1.0 HH B:TYR140 4.3 23.8 1.0 HD11 B:LEU117 4.3 28.7 1.0 C3B B:HEM503 4.3 18.2 1.0 C2C B:HEM503 4.3 16.7 1.0 HD11 B:LEU144 4.3 23.1 1.0 HHD B:HEM503 4.4 22.4 1.0 HHB B:HEM503 4.4 21.0 1.0 HHA B:HEM503 4.5 29.3 1.0 CE2 B:PHE78 4.5 18.0 1.0 HHC B:HEM503 4.6 24.2 1.0 CD1 B:LEU144 4.6 19.2 1.0 CZ B:PHE78 4.6 22.0 1.0 HG3 B:PRO115 4.8 31.4 1.0 HG2 B:PRO115 5.0 31.4 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