Iron in PDB 1rse: Myoglobin (Horse Heart) Mutant with Ser 92 Replaced By Asp (S92D)

The structure of Myoglobin (Horse Heart) Mutant with Ser 92 Replaced By Asp (S92D), PDB code: 1rse was solved by D.L.Burk, G.D.Brayer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	6.00 / 1.70
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	64.420, 28.880, 35.970, 90.00, 107.00, 90.00
R / Rfree (%)	18.8 / n/a

The binding sites of Iron atom in the Myoglobin (Horse Heart) Mutant with Ser 92 Replaced By Asp (S92D) (pdb code 1rse). 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 Myoglobin (Horse Heart) Mutant with Ser 92 Replaced By Asp (S92D), PDB code: 1rse:

Iron binding site 1 out of 1 in the Myoglobin (Horse Heart) Mutant with Ser 92 Replaced By Asp (S92D)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Myoglobin (Horse Heart) Mutant with Ser 92 Replaced By Asp (S92D) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe154 b:14.6 occ:1.00 FE A:HEM154 0.0 14.6 1.0 ND A:HEM154 2.0 15.4 1.0 NA A:HEM154 2.0 14.7 1.0 NB A:HEM154 2.0 14.8 1.0 NC A:HEM154 2.0 13.9 1.0 NE2 A:HIS93 2.1 13.3 1.0 O A:HOH156 2.3 13.9 1.0 CE1 A:HIS93 3.0 14.1 1.0 C4C A:HEM154 3.0 12.6 1.0 C4A A:HEM154 3.0 14.0 1.0 C1D A:HEM154 3.0 14.6 1.0 C1A A:HEM154 3.0 16.0 1.0 C4D A:HEM154 3.0 16.5 1.0 C1C A:HEM154 3.1 13.0 1.0 C4B A:HEM154 3.1 13.4 1.0 C1B A:HEM154 3.1 13.8 1.0 CD2 A:HIS93 3.2 15.4 1.0 CHD A:HEM154 3.4 13.5 1.0 CHB A:HEM154 3.4 12.9 1.0 CHA A:HEM154 3.4 16.2 1.0 CHC A:HEM154 3.5 13.7 1.0 ND1 A:HIS93 4.2 16.0 1.0 CG A:HIS93 4.3 15.2 1.0 C2D A:HEM154 4.3 17.0 1.0 C3D A:HEM154 4.3 17.9 1.0 C2A A:HEM154 4.3 16.9 1.0 C3C A:HEM154 4.3 13.9 1.0 C3A A:HEM154 4.3 15.7 1.0 C2C A:HEM154 4.3 12.9 1.0 C3B A:HEM154 4.3 13.7 1.0 C2B A:HEM154 4.3 14.3 1.0 NE2 A:HIS64 4.5 14.3 1.0 CG2 A:VAL68 4.8 13.4 1.0 CE1 A:HIS64 4.9 15.2 1.0

E.Lloyd, D.L.Burk, J.C.Ferrer, R.Maurus, J.Doran, P.R.Carey, G.D.Brayer, A.G.Mauk. Electrostatic Modification of the Active Site of Myoglobin: Characterization of the Proximal SER92ASP Variant. Biochemistry V. 35 11901 1996.
ISSN: ISSN 0006-2960
PubMed: 8794773
DOI: 10.1021/BI9608976