Iron in PDB 1d06: Structural Basis of Dimerization and Sensory Mechanisms of Oxygen- Sensing Domain of Rhizobium Meliloti Fixl Determined at 1.4A Resolution

The structure of Structural Basis of Dimerization and Sensory Mechanisms of Oxygen- Sensing Domain of Rhizobium Meliloti Fixl Determined at 1.4A Resolution, PDB code: 1d06 was solved by H.Miyatake, M.Mukai, S.-Y.Park, S.Adachi, K.Tamura, H.Nakamura, K.Nakamura, T.Tsuchiya, T.Iizuka, Y.Shiro, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.40
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	60.600, 37.150, 53.990, 90.00, 115.43, 90.00
R / Rfree (%)	22.4 / 27.5

The binding sites of Iron atom in the Structural Basis of Dimerization and Sensory Mechanisms of Oxygen- Sensing Domain of Rhizobium Meliloti Fixl Determined at 1.4A Resolution (pdb code 1d06). 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 Structural Basis of Dimerization and Sensory Mechanisms of Oxygen- Sensing Domain of Rhizobium Meliloti Fixl Determined at 1.4A Resolution, PDB code: 1d06:

Iron binding site 1 out of 1 in the Structural Basis of Dimerization and Sensory Mechanisms of Oxygen- Sensing Domain of Rhizobium Meliloti Fixl Determined at 1.4A Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structural Basis of Dimerization and Sensory Mechanisms of Oxygen- Sensing Domain of Rhizobium Meliloti Fixl Determined at 1.4A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:7.9 occ:1.00 FE A:HEM501 0.0 7.9 1.0 ND A:HEM501 2.0 8.1 1.0 NA A:HEM501 2.0 7.6 1.0 NB A:HEM501 2.0 8.4 1.0 NC A:HEM501 2.0 8.3 1.0 NE2 A:HIS194 2.1 9.9 1.0 C1A A:HEM501 3.0 10.7 1.0 C4D A:HEM501 3.0 10.1 1.0 C1C A:HEM501 3.1 7.5 1.0 C4A A:HEM501 3.1 9.8 1.0 C1B A:HEM501 3.1 8.4 1.0 C1D A:HEM501 3.1 8.5 1.0 C4B A:HEM501 3.1 7.8 1.0 C4C A:HEM501 3.1 7.5 1.0 CE1 A:HIS194 3.1 9.7 1.0 CD2 A:HIS194 3.1 10.1 1.0 CHB A:HEM501 3.4 9.0 1.0 CHC A:HEM501 3.4 9.9 1.0 CHA A:HEM501 3.5 10.8 1.0 CHD A:HEM501 3.5 7.4 1.0 CD2 A:LEU230 4.0 11.2 1.0 ND1 A:HIS194 4.3 10.8 1.0 C3D A:HEM501 4.3 9.8 1.0 C2A A:HEM501 4.3 12.4 1.0 C2B A:HEM501 4.3 8.5 1.0 C3A A:HEM501 4.3 11.5 1.0 C2D A:HEM501 4.3 9.9 1.0 CG A:HIS194 4.3 11.6 1.0 C2C A:HEM501 4.3 7.8 1.0 C3B A:HEM501 4.3 7.7 1.0 C3C A:HEM501 4.4 7.3 1.0 CE A:MET186 4.8 11.7 1.0 CG1 A:VAL232 4.9 14.4 1.0

H.Miyatake, M.Mukai, S.-Y.Park, S.Adachi, K.Tamura, H.Nakamura, K.Nakamura, T.Tsuchiya, T.Iizuka, Y.Shiro. Sensory Mechanism of Oxygen Sensor Fixl From Rhizobium Meliloti: Crystallographic, Mutagenesis and Resonance Raman Spectroscopic Studies J.Mol.Biol. V. 301 415 2000.
ISSN: ISSN 0022-2836
PubMed: 10926518
DOI: 10.1006/JMBI.2000.3954