Iron in PDB 1dtm: Crystal Structure of the Sperm-Whale Myoglobin Mutant H93G Complexed with 4-Methylimidazole, Metaquo Form

The structure of Crystal Structure of the Sperm-Whale Myoglobin Mutant H93G Complexed with 4-Methylimidazole, Metaquo Form, PDB code: 1dtm 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 / 2.13
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	40.276, 48.892, 78.935, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Iron atom in the Crystal Structure of the Sperm-Whale Myoglobin Mutant H93G Complexed with 4-Methylimidazole, Metaquo Form (pdb code 1dtm). 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 the Sperm-Whale Myoglobin Mutant H93G Complexed with 4-Methylimidazole, Metaquo Form, PDB code: 1dtm:

Iron binding site 1 out of 1 in the Crystal Structure of the Sperm-Whale Myoglobin Mutant H93G Complexed with 4-Methylimidazole, Metaquo Form


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 the Sperm-Whale Myoglobin Mutant H93G Complexed with 4-Methylimidazole, Metaquo Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe154 b:26.0 occ:1.00 FE A:HEM154 0.0 26.0 1.0 NC A:HEM154 1.7 11.7 1.0 NA A:HEM154 1.8 9.4 1.0 ND A:HEM154 1.9 19.9 1.0 NE2 A:4MZ155 2.0 37.8 1.0 NB A:HEM154 2.0 11.8 1.0 C4C A:HEM154 2.7 37.5 1.0 O A:HOH156 2.7 17.5 1.0 C1A A:HEM154 2.9 23.0 1.0 C4A A:HEM154 2.9 1.2 1.0 C1D A:HEM154 2.9 26.5 1.0 C1C A:HEM154 2.9 14.2 1.0 CD2 A:4MZ155 2.9 18.4 1.0 C4D A:HEM154 3.0 25.1 1.0 CE1 A:4MZ155 3.0 34.8 1.0 C1B A:HEM154 3.1 1.0 1.0 C4B A:HEM154 3.1 3.0 1.0 CHD A:HEM154 3.2 2.3 1.0 CHA A:HEM154 3.4 20.0 1.0 CHB A:HEM154 3.4 13.1 1.0 CHC A:HEM154 3.5 15.5 1.0 C3C A:HEM154 4.0 8.3 1.0 C2C A:HEM154 4.1 12.4 1.0 C3A A:HEM154 4.1 36.1 1.0 C2A A:HEM154 4.1 24.2 1.0 CG A:4MZ155 4.1 15.5 1.0 ND1 A:4MZ155 4.1 19.9 1.0 C2D A:HEM154 4.2 25.4 1.0 C3D A:HEM154 4.2 23.1 1.0 C2B A:HEM154 4.3 13.3 1.0 C3B A:HEM154 4.3 5.4 1.0 CE1 A:HIS64 4.4 50.5 1.0 NE2 A:HIS64 4.5 50.4 1.0 CG2 A:VAL68 4.9 10.2 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