Iron in PDB 3rgk: Crystal Structure of Human Myoglobin Mutant K45R

The structure of Crystal Structure of Human Myoglobin Mutant K45R, PDB code: 3rgk was solved by S.R.Hubbard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	18.40 / 1.65
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	86.200, 86.200, 35.660, 90.00, 90.00, 120.00
R / Rfree (%)	17.5 / 19.8

The binding sites of Iron atom in the Crystal Structure of Human Myoglobin Mutant K45R (pdb code 3rgk). 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 Crystal Structure of Human Myoglobin Mutant K45R, PDB code: 3rgk:

Iron binding site 1 out of 1 in the Crystal Structure of Human Myoglobin Mutant K45R


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 Human Myoglobin Mutant K45R within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe154 b:7.8 occ:1.00 FE A:HEM154 0.0 7.8 1.0 NA A:HEM154 2.1 6.7 1.0 NC A:HEM154 2.1 7.0 1.0 NB A:HEM154 2.1 6.9 1.0 ND A:HEM154 2.1 7.2 1.0 O A:HOH200 2.1 10.3 1.0 NE2 A:HIS93 2.2 7.5 1.0 C1D A:HEM154 3.1 7.3 1.0 C4A A:HEM154 3.1 7.4 1.0 C4C A:HEM154 3.1 6.7 1.0 C1C A:HEM154 3.1 5.5 1.0 C1A A:HEM154 3.1 7.6 1.0 C4B A:HEM154 3.1 6.4 1.0 C1B A:HEM154 3.1 7.2 1.0 C4D A:HEM154 3.1 7.6 1.0 CE1 A:HIS93 3.1 7.2 1.0 CD2 A:HIS93 3.2 7.6 1.0 CHD A:HEM154 3.4 8.0 1.0 CHC A:HEM154 3.4 7.7 1.0 CHB A:HEM154 3.4 7.0 1.0 CHA A:HEM154 3.4 7.7 1.0 ND1 A:HIS93 4.2 8.0 1.0 C3A A:HEM154 4.3 7.5 1.0 C2C A:HEM154 4.3 6.2 1.0 C3C A:HEM154 4.3 7.0 1.0 CG A:HIS93 4.3 7.6 1.0 C2A A:HEM154 4.3 8.0 1.0 C3B A:HEM154 4.3 6.6 1.0 C2B A:HEM154 4.3 6.7 1.0 C2D A:HEM154 4.3 7.8 1.0 C3D A:HEM154 4.3 8.5 1.0 NE2 A:HIS64 4.5 10.5 1.0 CG2 A:VAL68 4.8 8.3 1.0 CE1 A:HIS64 5.0 11.7 1.0

S.R.Hubbard, S.G.Lambright, S.G.Boxer, W.A.Hendrickson. X-Ray Crystal Structure of A Recombinant Human Myoglobin Mutant at 2.8 A Resolution J.Mol.Biol. V. 20 215 1990.
ISSN: ISSN 0022-2836
PubMed: 2342104