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Iron in PDB 1nz2: K45E Variant of Horse Heart Myoglobin

Protein crystallography data

The structure of K45E Variant of Horse Heart Myoglobin, PDB code: 1nz2 was solved by C.L.Hunter, R.Maurus, M.R.Mauk, H.Lee, E.L.Raven, H.Tong, N.Nguyen, M.Smith, G.D.Brayer, A.G.Mauk, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.90
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 64.200, 28.800, 35.900, 90.00, 107.10, 90.00
R / Rfree (%) n/a / n/a

Iron Binding Sites:

The binding sites of Iron atom in the K45E Variant of Horse Heart Myoglobin (pdb code 1nz2). 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 K45E Variant of Horse Heart Myoglobin, PDB code: 1nz2:

Iron binding site 1 out of 1 in 1nz2

Go back to Iron Binding Sites List in 1nz2
Iron binding site 1 out of 1 in the K45E Variant of Horse Heart Myoglobin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of K45E Variant of Horse Heart Myoglobin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe154

b:12.5
occ:1.00
FE A:HEM154 0.0 12.5 1.0
NB A:HEM154 2.0 11.0 1.0
ND A:HEM154 2.0 12.8 1.0
NC A:HEM154 2.0 11.1 1.0
NA A:HEM154 2.0 10.9 1.0
NE2 A:HIS93 2.1 9.9 1.0
O A:HOH156 2.2 9.9 1.0
C4A A:HEM154 3.0 10.6 1.0
C4C A:HEM154 3.0 10.7 1.0
C1B A:HEM154 3.0 10.5 1.0
C1C A:HEM154 3.0 9.6 1.0
C4B A:HEM154 3.0 10.6 1.0
C1A A:HEM154 3.1 10.1 1.0
C4D A:HEM154 3.1 12.2 1.0
C1D A:HEM154 3.1 12.1 1.0
CD2 A:HIS93 3.1 10.6 1.0
CE1 A:HIS93 3.1 13.0 1.0
CHC A:HEM154 3.4 10.6 1.0
CHB A:HEM154 3.4 9.3 1.0
CHD A:HEM154 3.5 8.7 1.0
CHA A:HEM154 3.5 9.8 1.0
CG A:HIS93 4.2 12.3 1.0
ND1 A:HIS93 4.2 12.7 1.0
C2B A:HEM154 4.3 12.1 1.0
C3B A:HEM154 4.3 11.9 1.0
C3A A:HEM154 4.3 10.5 1.0
C2A A:HEM154 4.3 8.1 1.0
C2C A:HEM154 4.3 10.9 1.0
C3C A:HEM154 4.3 11.0 1.0
C2D A:HEM154 4.3 13.4 1.0
C3D A:HEM154 4.3 13.0 1.0
NE2 A:HIS64 4.4 10.0 1.0
CG2 A:VAL68 4.8 7.7 1.0
CE1 A:HIS64 4.9 12.6 1.0

Reference:

C.L.Hunter, R.Maurus, M.R.Mauk, H.Lee, E.L.Raven, H.Tong, N.Nguyen, M.Smith, G.D.Brayer, A.G.Mauk. Introduction and Characterization of A Functionally Linked Metal Ion Binding Site at the Exposed Heme Edge of Myoglobin Proc.Natl.Acad.Sci.Usa V. 100 3647 2003.
ISSN: ISSN 0027-8424
PubMed: 12644706
DOI: 10.1073/PNAS.0636702100
Page generated: Sat Aug 3 12:05:36 2024

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