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Iron in PDB 1dti: Recombinant Sperm Whale Myoglobin H97D, D122N Mutant (Met)

Protein crystallography data

The structure of Recombinant Sperm Whale Myoglobin H97D, D122N Mutant (Met), PDB code: 1dti was solved by E.C.Liong, G.N.Phillips Jr., with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 5.00 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 49.163, 40.002, 80.011, 90.00, 90.00, 90.00
R / Rfree (%) 18.3 / 22.8

Iron Binding Sites:

The binding sites of Iron atom in the Recombinant Sperm Whale Myoglobin H97D, D122N Mutant (Met) (pdb code 1dti). 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 Recombinant Sperm Whale Myoglobin H97D, D122N Mutant (Met), PDB code: 1dti:

Iron binding site 1 out of 1 in 1dti

Go back to Iron Binding Sites List in 1dti
Iron binding site 1 out of 1 in the Recombinant Sperm Whale Myoglobin H97D, D122N Mutant (Met)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Recombinant Sperm Whale Myoglobin H97D, D122N Mutant (Met) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe154

b:17.4
occ:1.00
FE A:HEM154 0.0 17.4 1.0
ND A:HEM154 1.9 16.4 1.0
NA A:HEM154 1.9 15.8 1.0
NC A:HEM154 1.9 18.0 1.0
NB A:HEM154 2.0 14.1 1.0
NE2 A:HIS93 2.1 13.4 1.0
O A:HOH155 2.2 17.1 1.0
C1D A:HEM154 3.0 16.2 1.0
C4D A:HEM154 3.0 15.6 1.0
C1A A:HEM154 3.0 12.1 1.0
C4C A:HEM154 3.0 16.4 1.0
C4A A:HEM154 3.0 11.3 1.0
C1B A:HEM154 3.0 13.6 1.0
C4B A:HEM154 3.0 12.5 1.0
C1C A:HEM154 3.0 15.5 1.0
CD2 A:HIS93 3.1 23.0 1.0
CE1 A:HIS93 3.1 25.1 1.0
CHA A:HEM154 3.3 14.5 1.0
CHD A:HEM154 3.3 16.3 1.0
CHB A:HEM154 3.3 10.1 1.0
CHC A:HEM154 3.3 10.9 1.0
ND1 A:HIS93 4.2 21.1 1.0
CG A:HIS93 4.3 18.1 1.0
C3D A:HEM154 4.3 21.6 1.0
C2D A:HEM154 4.3 23.4 1.0
C2A A:HEM154 4.3 17.3 1.0
C3A A:HEM154 4.3 18.0 1.0
C2B A:HEM154 4.3 18.3 1.0
C2C A:HEM154 4.3 16.6 1.0
C3C A:HEM154 4.3 16.0 1.0
C3B A:HEM154 4.3 15.2 1.0
NE2 A:HIS64 4.4 19.0 1.0
CE1 A:HIS64 4.8 22.7 1.0
CG2 A:VAL68 4.9 17.4 1.0

Reference:

E.C.Liong, Y.Dou, E.E.Scott, J.S.Olson, G.N.Phillips Jr.. Waterproofing the Heme Pocket. Role of Proximal Amino Acid Side Chains in Preventing Hemin Loss From Myoglobin. J.Biol.Chem. V. 276 9093 2001.
ISSN: ISSN 0021-9258
PubMed: 11084036
DOI: 10.1074/JBC.M008593200
Page generated: Wed Jul 16 13:25:41 2025

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