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Iron in PDB 2vcn: Structure of Isoniazid (Inh) Bound to Cytosolic Soybean Ascorbate Peroxidase Mutant W41A

Enzymatic activity of Structure of Isoniazid (Inh) Bound to Cytosolic Soybean Ascorbate Peroxidase Mutant W41A

All present enzymatic activity of Structure of Isoniazid (Inh) Bound to Cytosolic Soybean Ascorbate Peroxidase Mutant W41A:
1.11.1.11;

Protein crystallography data

The structure of Structure of Isoniazid (Inh) Bound to Cytosolic Soybean Ascorbate Peroxidase Mutant W41A, PDB code: 2vcn 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) 36.74 / 1.20
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 82.126, 82.126, 75.160, 90.00, 90.00, 90.00
R / Rfree (%) 21.2 / 23

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Isoniazid (Inh) Bound to Cytosolic Soybean Ascorbate Peroxidase Mutant W41A (pdb code 2vcn). 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 W41A, PDB code: 2vcn:

Iron binding site 1 out of 1 in 2vcn

Go back to Iron Binding Sites List in 2vcn
Iron binding site 1 out of 1 in the Structure of Isoniazid (Inh) Bound to Cytosolic Soybean Ascorbate Peroxidase Mutant W41A


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 W41A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1251

b:9.9
occ:1.00
 FE A:HEM1251 0.0 9.9 1.0
N3 A:ISZ1254 1.9 7.0 0.7
NA A:HEM1251 1.9 8.3 1.0
NC A:HEM1251 2.0 8.8 1.0
NE2 A:HIS163 2.1 7.6 1.0
ND A:HEM1251 2.1 8.8 1.0
NB A:HEM1251 2.1 8.7 1.0
O A:HOH2201 2.8 0.5 0.3
N2 A:ISZ1254 2.8 10.3 0.7
C1C A:HEM1251 3.0 8.8 1.0
C1A A:HEM1251 3.0 8.2 1.0
C4A A:HEM1251 3.0 8.9 1.0
CD2 A:HIS163 3.0 7.7 1.0
C4C A:HEM1251 3.0 7.7 1.0
CE1 A:HIS163 3.1 7.7 1.0
C4D A:HEM1251 3.1 7.6 1.0
C4B A:HEM1251 3.1 9.0 1.0
C1B A:HEM1251 3.1 10.2 1.0
C1D A:HEM1251 3.1 8.2 1.0
CHC A:HEM1251 3.4 8.3 1.0
CHA A:HEM1251 3.4 8.0 1.0
CHB A:HEM1251 3.4 8.9 1.0
CHD A:HEM1251 3.4 7.5 1.0
C6 A:ISZ1254 3.7 11.4 0.7
O1 A:ISZ1254 4.0 10.2 0.7
ND1 A:HIS163 4.2 8.9 1.0
CG A:HIS163 4.2 8.9 1.0
C2A A:HEM1251 4.2 8.1 1.0
C3A A:HEM1251 4.2 8.1 1.0
C2C A:HEM1251 4.2 8.4 1.0
C3C A:HEM1251 4.2 8.1 1.0
C2B A:HEM1251 4.3 8.9 1.0
C3D A:HEM1251 4.3 8.6 1.0
C3B A:HEM1251 4.3 9.1 1.0
C2D A:HEM1251 4.3 8.1 1.0
O A:HOH2040 4.4 14.2 1.0
O A:HOH2202 4.6 75.8 1.0
C1 A:ISZ1254 4.9 12.4 0.7

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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