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Iron in PDB 2v23: Structure of Cytochrome C Peroxidase Mutant N184R Y36A

Enzymatic activity of Structure of Cytochrome C Peroxidase Mutant N184R Y36A

All present enzymatic activity of Structure of Cytochrome C Peroxidase Mutant N184R Y36A:
1.11.1.5;

Protein crystallography data

The structure of Structure of Cytochrome C Peroxidase Mutant N184R Y36A, PDB code: 2v23 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) 61.66 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 51.146, 75.377, 107.228, 90.00, 90.00, 90.00
R / Rfree (%) 15.9 / 19.2

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Cytochrome C Peroxidase Mutant N184R Y36A (pdb code 2v23). 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 Cytochrome C Peroxidase Mutant N184R Y36A, PDB code: 2v23:

Iron binding site 1 out of 1 in 2v23

Go back to Iron Binding Sites List in 2v23
Iron binding site 1 out of 1 in the Structure of Cytochrome C Peroxidase Mutant N184R Y36A


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Cytochrome C Peroxidase Mutant N184R Y36A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1295

b:12.8
occ:1.00
FE A:HEM1295 0.0 12.8 1.0
NA A:HEM1295 2.1 10.8 1.0
NC A:HEM1295 2.1 10.9 1.0
NB A:HEM1295 2.1 10.2 1.0
NE2 A:HIS175 2.1 11.7 1.0
ND A:HEM1295 2.2 10.3 1.0
O A:HOH2078 2.6 36.7 1.0
C1C A:HEM1295 3.1 9.9 1.0
C4B A:HEM1295 3.1 9.6 1.0
C1A A:HEM1295 3.1 10.2 1.0
C4C A:HEM1295 3.1 9.5 1.0
C4A A:HEM1295 3.1 10.0 1.0
CE1 A:HIS175 3.1 10.6 1.0
CD2 A:HIS175 3.1 10.1 1.0
C1D A:HEM1295 3.1 9.7 1.0
C1B A:HEM1295 3.1 10.4 1.0
C4D A:HEM1295 3.1 9.0 1.0
CHC A:HEM1295 3.4 8.8 1.0
CHD A:HEM1295 3.4 9.0 1.0
CHA A:HEM1295 3.5 9.4 1.0
CHB A:HEM1295 3.5 9.7 1.0
NE1 A:TRP51 4.1 9.9 1.0
O A:HOH2081 4.1 17.3 1.0
ND1 A:HIS175 4.2 10.2 1.0
CG A:HIS175 4.3 10.1 1.0
NE A:ARG48 4.3 15.9 1.0
C2C A:HEM1295 4.3 10.1 1.0
C2A A:HEM1295 4.3 10.0 1.0
C3B A:HEM1295 4.3 9.7 1.0
C3A A:HEM1295 4.3 9.8 1.0
C3C A:HEM1295 4.3 9.3 1.0
C2B A:HEM1295 4.3 9.6 1.0
C2D A:HEM1295 4.3 9.5 1.0
C3D A:HEM1295 4.4 8.7 1.0
CD1 A:TRP51 4.6 10.1 1.0
NH2 A:ARG48 4.7 14.7 1.0
CH2 A:TRP191 5.0 12.0 1.0

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 02:33:07 2024

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