Iron in PDB 1duo: Sperm Whale Metaquomyoglobin Proximal Histidine Mutant H93G with 1- Methylimidazole As Proximal Ligand.

The structure of Sperm Whale Metaquomyoglobin Proximal Histidine Mutant H93G with 1- Methylimidazole As Proximal Ligand., PDB code: 1duo was solved by D.Barrick, F.W.Dahlquist, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	40.161, 49.033, 79.240, 90.00, 90.00, 90.00
R / Rfree (%)	18.1 / n/a

The binding sites of Iron atom in the Sperm Whale Metaquomyoglobin Proximal Histidine Mutant H93G with 1- Methylimidazole As Proximal Ligand. (pdb code 1duo). 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 Sperm Whale Metaquomyoglobin Proximal Histidine Mutant H93G with 1- Methylimidazole As Proximal Ligand., PDB code: 1duo:

Iron binding site 1 out of 1 in the Sperm Whale Metaquomyoglobin Proximal Histidine Mutant H93G with 1- Methylimidazole As Proximal Ligand.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Sperm Whale Metaquomyoglobin Proximal Histidine Mutant H93G with 1- Methylimidazole As Proximal Ligand. within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe154 b:16.6 occ:1.00 FE A:HEM154 0.0 16.6 1.0 NA A:HEM154 1.8 10.0 1.0 ND A:HEM154 1.9 12.3 1.0 NC A:HEM154 2.0 10.8 1.0 NB A:HEM154 2.0 8.7 1.0 N3 A:1MZ155 2.1 25.9 1.0 O A:HOH156 2.2 16.2 1.0 C2 A:1MZ155 2.9 15.1 1.0 C1A A:HEM154 2.9 4.9 1.0 C1D A:HEM154 2.9 15.7 1.0 C4D A:HEM154 2.9 15.9 1.0 C4A A:HEM154 3.0 5.5 1.0 C4B A:HEM154 3.0 2.6 1.0 C1C A:HEM154 3.0 28.1 1.0 C4C A:HEM154 3.0 20.2 1.0 C1B A:HEM154 3.1 6.3 1.0 C4 A:1MZ155 3.3 46.9 1.0 CHA A:HEM154 3.4 7.8 1.0 CHD A:HEM154 3.4 8.2 1.0 CHC A:HEM154 3.4 7.3 1.0 CHB A:HEM154 3.5 2.2 1.0 C2A A:HEM154 4.1 22.6 1.0 N1 A:1MZ155 4.1 22.7 1.0 C3A A:HEM154 4.1 7.1 1.0 C3D A:HEM154 4.1 27.4 1.0 C2D A:HEM154 4.1 38.1 1.0 C2C A:HEM154 4.2 8.5 1.0 C3C A:HEM154 4.3 13.0 1.0 C3B A:HEM154 4.3 4.8 1.0 C2B A:HEM154 4.3 9.7 1.0 C5 A:1MZ155 4.3 27.6 1.0 NE2 A:HIS64 4.4 21.7 1.0 CE1 A:HIS64 4.5 22.8 1.0 CG2 A:VAL68 4.6 6.6 1.0

D.Barrick, F.W.Dahlquist. Trans-Substitution of the Proximal Hydrogen Bond in Myoglobin: I. Structural Consequences of Hydrogen Bond Deletion. Proteins V. 39 278 2000.
ISSN: ISSN 0887-3585
PubMed: 10813811
DOI: 10.1002/(SICI)1097-0134(20000601)39:4<278::AID-PROT20>3.0.CO;2-T