Atomistry » Iron » PDB 1ds1-1dxr » 1dtm
Atomistry »
  Iron »
    PDB 1ds1-1dxr »
      1dtm »

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

Protein crystallography data

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

Iron Binding Sites:

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 1dtm

Go back to Iron Binding Sites List in 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

Reference:

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
Page generated: Wed Jul 16 13:25:47 2025

Last articles

Fe in 2YXO
Fe in 2YRS
Fe in 2YXC
Fe in 2YNM
Fe in 2YVJ
Fe in 2YP1
Fe in 2YU2
Fe in 2YU1
Fe in 2YQB
Fe in 2YOO
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy