Iron in PDB 2nrm: S-Nitrosylated Blackfin Tuna Myoglobin

The structure of S-Nitrosylated Blackfin Tuna Myoglobin, PDB code: 2nrm was solved by E.R.Schreiter, M.M.Rodr Guez, A.Weichsel, W.R.Montfort, J.Bonaventura, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.09
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	33.943, 51.932, 38.899, 90.00, 103.75, 90.00
R / Rfree (%)	13.3 / 15.7

The binding sites of Iron atom in the S-Nitrosylated Blackfin Tuna Myoglobin (pdb code 2nrm). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the S-Nitrosylated Blackfin Tuna Myoglobin, PDB code: 2nrm:

Iron binding site 1 out of 1 in the S-Nitrosylated Blackfin Tuna Myoglobin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of S-Nitrosylated Blackfin Tuna Myoglobin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe148 b:6.2 occ:1.00 FE A:HEM148 0.0 6.2 1.0 ND A:HEM148 2.0 5.7 1.0 NB A:HEM148 2.0 6.2 1.0 NA A:HEM148 2.0 5.9 1.0 NC A:HEM148 2.0 5.6 1.0 NE2 A:HIS89 2.1 6.0 1.0 O A:HOH305 2.1 7.1 1.0 C4A A:HEM148 3.0 6.1 1.0 CE1 A:HIS89 3.0 7.2 1.0 C1D A:HEM148 3.0 5.8 1.0 C1B A:HEM148 3.1 6.1 1.0 C4C A:HEM148 3.1 5.8 1.0 C4B A:HEM148 3.1 6.5 1.0 C4D A:HEM148 3.1 6.5 1.0 C1A A:HEM148 3.1 6.1 1.0 C1C A:HEM148 3.1 6.3 1.0 CD2 A:HIS89 3.1 5.8 1.0 CHD A:HEM148 3.4 6.0 1.0 CHC A:HEM148 3.4 6.7 1.0 CHB A:HEM148 3.4 6.6 1.0 CHA A:HEM148 3.4 6.3 1.0 ND1 A:HIS89 4.2 7.6 1.0 CG A:HIS89 4.2 5.7 1.0 NE2 A:HIS60 4.3 7.1 1.0 C2D A:HEM148 4.3 6.1 1.0 C3C A:HEM148 4.3 6.5 1.0 C3B A:HEM148 4.3 6.9 1.0 C3A A:HEM148 4.3 7.2 1.0 C3D A:HEM148 4.3 6.8 1.0 C2B A:HEM148 4.3 7.2 1.0 C2A A:HEM148 4.3 6.8 1.0 C2C A:HEM148 4.3 6.6 1.0 CG2 A:VAL64 4.7 7.6 1.0 CE1 A:HIS60 4.8 7.7 1.0

E.R.Schreiter, M.M.Rodriguez, A.Weichsel, W.R.Montfort, J.Bonaventura. S-Nitrosylation-Induced Conformational Change in Blackfin Tuna Myoglobin. J.Biol.Chem. V. 282 19773 2007.
ISSN: ISSN 0021-9258
PubMed: 17488722
DOI: 10.1074/JBC.M701363200