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Iron in PDB 2oz0: Mechanistic and Structural Studies of H373Q Flavocytochrome B2: Effects of Mutating the Active Site Base

Enzymatic activity of Mechanistic and Structural Studies of H373Q Flavocytochrome B2: Effects of Mutating the Active Site Base

All present enzymatic activity of Mechanistic and Structural Studies of H373Q Flavocytochrome B2: Effects of Mutating the Active Site Base:
1.1.2.3;

Protein crystallography data

The structure of Mechanistic and Structural Studies of H373Q Flavocytochrome B2: Effects of Mutating the Active Site Base, PDB code: 2oz0 was solved by C.-L.Tsai, K.Gokulan, P.Sobrado, J.C.Sacchettini, P.F.Fitzpatrick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.80
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 163.689, 163.689, 112.021, 90.00, 90.00, 120.00
R / Rfree (%) 20.6 / 27.8

Iron Binding Sites:

The binding sites of Iron atom in the Mechanistic and Structural Studies of H373Q Flavocytochrome B2: Effects of Mutating the Active Site Base (pdb code 2oz0). 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 Mechanistic and Structural Studies of H373Q Flavocytochrome B2: Effects of Mutating the Active Site Base, PDB code: 2oz0:

Iron binding site 1 out of 1 in 2oz0

Go back to Iron Binding Sites List in 2oz0
Iron binding site 1 out of 1 in the Mechanistic and Structural Studies of H373Q Flavocytochrome B2: Effects of Mutating the Active Site Base


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Mechanistic and Structural Studies of H373Q Flavocytochrome B2: Effects of Mutating the Active Site Base within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe560

b:97.1
occ:1.00
 FE A:HEM560 0.0 97.1 1.0
NE2 A:HIS66 1.8 0.1 1.0
NC A:HEM560 1.8 95.8 1.0
NB A:HEM560 1.9 94.9 1.0
NA A:HEM560 2.1 99.4 1.0
ND A:HEM560 2.2 97.9 1.0
NE2 A:HIS43 2.2 0.7 1.0
CE1 A:HIS66 2.6 0.5 1.0
CD2 A:HIS66 2.8 0.6 1.0
C4B A:HEM560 2.8 94.7 1.0
C4C A:HEM560 2.9 95.7 1.0
C1C A:HEM560 2.9 95.1 1.0
CE1 A:HIS43 2.9 0.6 1.0
C1B A:HEM560 3.0 96.8 1.0
C1D A:HEM560 3.1 98.7 1.0
C1A A:HEM560 3.1 0.5 1.0
C4A A:HEM560 3.2 0.9 1.0
CHC A:HEM560 3.2 95.8 1.0
CHD A:HEM560 3.2 97.9 1.0
CD2 A:HIS43 3.2 0.8 1.0
C4D A:HEM560 3.3 99.8 1.0
CHB A:HEM560 3.5 98.9 1.0
CHA A:HEM560 3.6 0.1 1.0
ND1 A:HIS66 3.7 0.1 1.0
CG A:HIS66 3.8 0.9 1.0
C3B A:HEM560 4.0 96.1 1.0
C2B A:HEM560 4.1 96.6 1.0
C3C A:HEM560 4.1 93.9 1.0
C2C A:HEM560 4.1 95.8 1.0
ND1 A:HIS43 4.1 0.1 1.0
CG A:HIS43 4.3 0.9 1.0
C3A A:HEM560 4.3 0.3 1.0
C2A A:HEM560 4.4 0.7 1.0
C2D A:HEM560 4.4 99.6 1.0
C3D A:HEM560 4.5 0.5 1.0
CD1 A:PHE62 4.9 0.4 1.0

Reference:

C.L.Tsai, K.Gokulan, P.Sobrado, J.C.Sacchettini, P.F.Fitzpatrick. Mechanistic and Structural Studies of H373Q Flavocytochrome B2: Effects of Mutating the Active Site Base. Biochemistry V. 46 7844 2007.
ISSN: ISSN 0006-2960
PubMed: 17563122
DOI: 10.1021/BI7005543
Page generated: Sun Aug 4 01:08:38 2024

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