Iron in PDB 1duk: Wild-Type Recombinant Sperm Whale Metaquomyoglobin

The structure of Wild-Type Recombinant Sperm Whale Metaquomyoglobin, PDB code: 1duk 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 (°)	40.132, 49.071, 79.339, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Iron atom in the Wild-Type Recombinant Sperm Whale Metaquomyoglobin (pdb code 1duk). 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 Wild-Type Recombinant Sperm Whale Metaquomyoglobin, PDB code: 1duk:

Iron binding site 1 out of 1 in the Wild-Type Recombinant Sperm Whale Metaquomyoglobin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Wild-Type Recombinant Sperm Whale Metaquomyoglobin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe155 b:15.4 occ:1.00 FE A:HEM155 0.0 15.4 1.0 ND A:HEM155 1.8 5.0 1.0 NA A:HEM155 1.9 5.0 1.0 NC A:HEM155 2.0 19.5 1.0 NB A:HEM155 2.0 5.0 1.0 NE2 A:HIS93 2.3 18.0 1.0 O A:HOH156 2.7 19.6 1.0 C4D A:HEM155 2.9 5.0 1.0 C1D A:HEM155 2.9 5.0 1.0 C1A A:HEM155 3.0 5.8 1.0 C4C A:HEM155 3.0 11.1 1.0 C4A A:HEM155 3.0 5.0 1.0 C1C A:HEM155 3.0 33.0 1.0 C4B A:HEM155 3.1 5.0 1.0 C1B A:HEM155 3.1 5.0 1.0 CD2 A:HIS93 3.2 18.7 1.0 CE1 A:HIS93 3.3 18.2 1.0 CHA A:HEM155 3.3 13.7 1.0 CHD A:HEM155 3.4 5.0 1.0 CHC A:HEM155 3.4 10.2 1.0 CHB A:HEM155 3.5 5.0 1.0 C3D A:HEM155 4.1 6.8 1.0 C2D A:HEM155 4.1 19.8 1.0 C2A A:HEM155 4.2 18.3 1.0 C3A A:HEM155 4.2 11.9 1.0 C3C A:HEM155 4.2 10.8 1.0 C2C A:HEM155 4.2 12.3 1.0 C3B A:HEM155 4.3 5.0 1.0 C2B A:HEM155 4.3 5.0 1.0 CG A:HIS93 4.4 19.8 1.0 ND1 A:HIS93 4.5 17.5 1.0 CE1 A:HIS64 4.8 14.7 1.0 NE2 A:HIS64 4.9 16.9 1.0 CG2 A:VAL68 4.9 5.0 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