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Iron in PDB 2vcs: Structure of Isoniazid (Inh) Bound to Cytosolic Soybean Ascorbate Peroxidase Mutant H42A

Enzymatic activity of Structure of Isoniazid (Inh) Bound to Cytosolic Soybean Ascorbate Peroxidase Mutant H42A

All present enzymatic activity of Structure of Isoniazid (Inh) Bound to Cytosolic Soybean Ascorbate Peroxidase Mutant H42A:
1.11.1.11;

Protein crystallography data

The structure of Structure of Isoniazid (Inh) Bound to Cytosolic Soybean Ascorbate Peroxidase Mutant H42A, PDB code: 2vcs was solved by C.L.Metcalfe, I.K.Macdonald, K.A.Brown, E.L.Raven, P.C.E.Moody, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.62 / 1.68
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 81.735, 81.735, 74.937, 90.00, 90.00, 90.00
R / Rfree (%) 16.6 / 21

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Isoniazid (Inh) Bound to Cytosolic Soybean Ascorbate Peroxidase Mutant H42A (pdb code 2vcs). 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 Structure of Isoniazid (Inh) Bound to Cytosolic Soybean Ascorbate Peroxidase Mutant H42A, PDB code: 2vcs:

Iron binding site 1 out of 1 in 2vcs

Go back to Iron Binding Sites List in 2vcs
Iron binding site 1 out of 1 in the Structure of Isoniazid (Inh) Bound to Cytosolic Soybean Ascorbate Peroxidase Mutant H42A


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Isoniazid (Inh) Bound to Cytosolic Soybean Ascorbate Peroxidase Mutant H42A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1251

b:13.7
occ:1.00
 FE A:HEM1251 0.0 13.7 1.0
NC A:HEM1251 2.0 11.3 1.0
NE2 A:HIS163 2.0 13.9 1.0
NB A:HEM1251 2.0 11.1 1.0
NA A:HEM1251 2.1 12.4 1.0
ND A:HEM1251 2.1 10.4 1.0
O A:HOH2295 2.4 18.1 0.1
C4B A:HEM1251 3.0 11.9 1.0
CD2 A:HIS163 3.0 11.3 1.0
C1C A:HEM1251 3.0 10.5 1.0
CE1 A:HIS163 3.0 12.3 1.0
C4C A:HEM1251 3.0 11.4 1.0
C1D A:HEM1251 3.1 11.4 1.0
C1B A:HEM1251 3.1 11.3 1.0
C1A A:HEM1251 3.1 12.5 1.0
C4D A:HEM1251 3.1 11.0 1.0
C4A A:HEM1251 3.1 11.3 1.0
CHC A:HEM1251 3.3 9.6 1.0
CHD A:HEM1251 3.4 11.7 1.0
CHA A:HEM1251 3.5 10.2 1.0
CHB A:HEM1251 3.5 11.6 1.0
N1 A:ISZ1252 3.7 25.3 0.9
C5 A:ISZ1252 3.9 24.8 0.9
NE1 A:TRP41 4.1 18.7 1.0
ND1 A:HIS163 4.1 14.1 1.0
CG A:HIS163 4.2 12.3 1.0
C3B A:HEM1251 4.3 12.2 1.0
C2C A:HEM1251 4.3 11.0 1.0
C3C A:HEM1251 4.3 11.2 1.0
C2B A:HEM1251 4.3 12.1 1.0
C2D A:HEM1251 4.3 11.4 1.0
C2A A:HEM1251 4.3 12.6 1.0
C3D A:HEM1251 4.3 11.8 1.0
C3A A:HEM1251 4.4 11.8 1.0
CD1 A:TRP41 4.4 16.7 1.0
C4 A:ISZ1252 4.6 25.2 0.9
C3 A:ISZ1252 4.9 24.9 0.9

Reference:

C.L.Metcalfe, I.K.Macdonald, E.J.Murphy, K.A.Brown, E.L.Raven, P.C.E.Moody. The Tuberculosis Prodrug Isoniazid Bound to Activating Peroxidases. J.Biol.Chem. V. 283 6193 2008.
ISSN: ISSN 0021-9258
PubMed: 18056997
DOI: 10.1074/JBC.M707412200
Page generated: Sun Aug 4 02:36:00 2024

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