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Iron in PDB 2oh8: Myoglobin Cavity Mutant I28W

Protein crystallography data

The structure of Myoglobin Cavity Mutant I28W, PDB code: 2oh8 was solved by G.N.Phillips Jr., J.Soman, J.S.Olson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.89 / 1.80
Space group P 6
Cell size a, b, c (Å), α, β, γ (°) 91.438, 91.438, 45.900, 90.00, 90.00, 120.00
R / Rfree (%) 15.6 / 18

Iron Binding Sites:

The binding sites of Iron atom in the Myoglobin Cavity Mutant I28W (pdb code 2oh8). 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 Myoglobin Cavity Mutant I28W, PDB code: 2oh8:

Iron binding site 1 out of 1 in 2oh8

Go back to Iron Binding Sites List in 2oh8
Iron binding site 1 out of 1 in the Myoglobin Cavity Mutant I28W


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Myoglobin Cavity Mutant I28W within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe154

b:9.3
occ:1.00
FE A:HEM154 0.0 9.3 1.0
NA A:HEM154 1.9 8.3 1.0
NC A:HEM154 2.0 8.2 1.0
ND A:HEM154 2.0 8.7 1.0
NB A:HEM154 2.0 8.8 1.0
O A:HOH202 2.1 9.5 1.0
NE2 A:HIS93 2.1 7.0 1.0
C1D A:HEM154 3.0 8.3 1.0
C4A A:HEM154 3.0 8.1 1.0
C1A A:HEM154 3.0 7.2 1.0
C4C A:HEM154 3.0 9.0 1.0
C4D A:HEM154 3.0 7.9 1.0
C1C A:HEM154 3.0 8.6 1.0
C1B A:HEM154 3.0 10.1 1.0
C4B A:HEM154 3.1 9.2 1.0
CE1 A:HIS93 3.1 11.0 1.0
CD2 A:HIS93 3.1 8.4 1.0
CHD A:HEM154 3.4 7.9 1.0
CHA A:HEM154 3.4 9.1 1.0
CHB A:HEM154 3.4 8.5 1.0
CHC A:HEM154 3.4 9.7 1.0
ND1 A:HIS93 4.2 8.4 1.0
C3A A:HEM154 4.2 8.8 1.0
C2D A:HEM154 4.2 10.3 1.0
C2A A:HEM154 4.2 9.9 1.0
C3C A:HEM154 4.2 10.8 1.0
C3D A:HEM154 4.2 8.8 1.0
C2C A:HEM154 4.2 11.2 1.0
CG A:HIS93 4.3 8.5 1.0
C2B A:HEM154 4.3 10.3 1.0
C3B A:HEM154 4.3 8.9 1.0
NE2 A:HIS64 4.4 9.3 1.0
CG2 A:VAL68 4.8 13.2 1.0
CE1 A:HIS64 4.9 12.1 1.0

Reference:

J.S.Olson, J.Soman, G.N.Phillips. Ligand Pathways in Myoglobin: A Review of Trp Cavity Mutations. Iubmb Life V. 59 552 2007.
ISSN: ISSN 1521-6543
PubMed: 17701550
DOI: 10.1080/15216540701230495
Page generated: Sun Aug 4 00:58:12 2024

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