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Iron in PDB 5utb: Met Form of Sperm Whale Myoglobin V68A/I107Y

Protein crystallography data

The structure of Met Form of Sperm Whale Myoglobin V68A/I107Y, PDB code: 5utb was solved by B.Wang, L.M.Thomas, G.B.Richter-Addo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.19 / 1.78
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 34.437, 30.778, 64.043, 90.00, 105.47, 90.00
R / Rfree (%) 16 / 19.9

Iron Binding Sites:

The binding sites of Iron atom in the Met Form of Sperm Whale Myoglobin V68A/I107Y (pdb code 5utb). 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 Met Form of Sperm Whale Myoglobin V68A/I107Y, PDB code: 5utb:

Iron binding site 1 out of 1 in 5utb

Go back to Iron Binding Sites List in 5utb
Iron binding site 1 out of 1 in the Met Form of Sperm Whale Myoglobin V68A/I107Y


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Met Form of Sperm Whale Myoglobin V68A/I107Y within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe201

b:16.4
occ:1.00
FE A:HEM201 0.0 16.4 1.0
ND A:HEM201 1.9 14.9 1.0
NA A:HEM201 2.0 15.1 1.0
NB A:HEM201 2.1 15.6 1.0
NC A:HEM201 2.1 15.1 1.0
NE2 A:HIS93 2.1 12.8 1.0
O A:HOH324 2.1 15.5 1.0
C1D A:HEM201 2.9 15.2 1.0
C4D A:HEM201 3.0 15.5 1.0
C4A A:HEM201 3.0 14.3 1.0
C1A A:HEM201 3.0 14.7 1.0
C1B A:HEM201 3.0 15.8 1.0
CE1 A:HIS93 3.0 14.5 1.0
C4C A:HEM201 3.1 14.5 1.0
C4B A:HEM201 3.1 17.7 1.0
C1C A:HEM201 3.1 15.4 1.0
CD2 A:HIS93 3.2 13.5 1.0
CHD A:HEM201 3.4 14.2 1.0
CHA A:HEM201 3.4 14.5 1.0
CHB A:HEM201 3.4 15.5 1.0
CHC A:HEM201 3.5 15.9 1.0
C2D A:HEM201 4.2 16.8 1.0
ND1 A:HIS93 4.2 15.2 1.0
C3D A:HEM201 4.2 16.8 1.0
C3A A:HEM201 4.2 15.9 1.0
C2A A:HEM201 4.2 15.6 1.0
C2C A:HEM201 4.3 16.8 1.0
NE2 A:HIS64 4.3 16.3 1.0
CG A:HIS93 4.3 13.7 1.0
C3C A:HEM201 4.3 16.2 1.0
C2B A:HEM201 4.3 18.4 1.0
C3B A:HEM201 4.4 18.9 1.0
CE1 A:HIS64 4.7 14.7 1.0

Reference:

B.Wang, Y.Shi, J.Tejero, S.M.Powell, L.M.Thomas, M.T.Gladwin, S.Shiva, Y.Zhang, G.B.Richter-Addo. Nitrosyl Myoglobins and Their Nitrite Precursors: Crystal Structural and Quantum Mechanics and Molecular Mechanics Theoretical Investigations of Preferred Fe -No Ligand Orientations in Myoglobin Distal Pockets. Biochemistry V. 57 4788 2018.
ISSN: ISSN 1520-4995
PubMed: 29999305
DOI: 10.1021/ACS.BIOCHEM.8B00542
Page generated: Tue Aug 6 10:02:47 2024

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