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Iron in PDB 5vzn: Wild-Type Sperm Whale Myoglobin with Nitric Oxide

Protein crystallography data

The structure of Wild-Type Sperm Whale Myoglobin with Nitric Oxide, PDB code: 5vzn 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) 26.42 / 1.70
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 34.800, 29.260, 63.949, 90.00, 105.79, 90.00
R / Rfree (%) 13.7 / 19

Iron Binding Sites:

The binding sites of Iron atom in the Wild-Type Sperm Whale Myoglobin with Nitric Oxide (pdb code 5vzn). 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 Sperm Whale Myoglobin with Nitric Oxide, PDB code: 5vzn:

Iron binding site 1 out of 1 in 5vzn

Go back to Iron Binding Sites List in 5vzn
Iron binding site 1 out of 1 in the Wild-Type Sperm Whale Myoglobin with Nitric Oxide


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Wild-Type Sperm Whale Myoglobin with Nitric Oxide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe201

b:10.0
occ:1.00
FE A:HEM201 0.0 10.0 1.0
N A:NO202 1.8 11.1 1.0
ND A:HEM201 2.0 9.7 1.0
NA A:HEM201 2.0 9.1 1.0
NC A:HEM201 2.1 9.3 1.0
NB A:HEM201 2.1 10.1 1.0
NE2 A:HIS93 2.2 10.9 1.0
O A:NO202 2.8 14.8 1.0
C1D A:HEM201 3.0 9.9 1.0
C4D A:HEM201 3.0 9.5 1.0
C1C A:HEM201 3.0 8.8 1.0
C1A A:HEM201 3.0 9.9 1.0
C4C A:HEM201 3.0 9.3 1.0
C4B A:HEM201 3.0 9.2 1.0
C1B A:HEM201 3.0 9.5 1.0
C4A A:HEM201 3.1 10.3 1.0
CE1 A:HIS93 3.1 11.3 1.0
CD2 A:HIS93 3.2 10.3 1.0
CHA A:HEM201 3.4 9.3 1.0
CHC A:HEM201 3.4 9.4 1.0
CHD A:HEM201 3.4 10.0 1.0
CHB A:HEM201 3.4 9.7 1.0
C2C A:HEM201 4.2 9.0 1.0
C3C A:HEM201 4.2 8.9 1.0
C2A A:HEM201 4.2 10.2 1.0
ND1 A:HIS93 4.3 11.5 1.0
C2B A:HEM201 4.3 9.4 1.0
C3A A:HEM201 4.3 10.1 1.0
C3B A:HEM201 4.3 10.4 1.0
C3D A:HEM201 4.3 10.8 1.0
C2D A:HEM201 4.3 9.9 1.0
CG A:HIS93 4.3 10.0 1.0
NE2 A:HIS64 4.4 11.4 1.0
CG2 A:VAL68 4.5 10.1 1.0
CE1 A:HIS64 4.9 11.4 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 11:04:20 2024

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