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Iron in PDB 2e39: Crystal Structure of the Cn-Bound Form of Arthromyces Ramosus Peroxidase at 1.3 Angstroms Resolution

Enzymatic activity of Crystal Structure of the Cn-Bound Form of Arthromyces Ramosus Peroxidase at 1.3 Angstroms Resolution

All present enzymatic activity of Crystal Structure of the Cn-Bound Form of Arthromyces Ramosus Peroxidase at 1.3 Angstroms Resolution:
1.11.1.7;

Protein crystallography data

The structure of Crystal Structure of the Cn-Bound Form of Arthromyces Ramosus Peroxidase at 1.3 Angstroms Resolution, PDB code: 2e39 was solved by K.Fukuyama, T.Okada, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.30
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 73.840, 73.840, 115.680, 90.00, 90.00, 90.00
R / Rfree (%) 15 / 20.3

Other elements in 2e39:

The structure of Crystal Structure of the Cn-Bound Form of Arthromyces Ramosus Peroxidase at 1.3 Angstroms Resolution also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the Cn-Bound Form of Arthromyces Ramosus Peroxidase at 1.3 Angstroms Resolution (pdb code 2e39). 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 Crystal Structure of the Cn-Bound Form of Arthromyces Ramosus Peroxidase at 1.3 Angstroms Resolution, PDB code: 2e39:

Iron binding site 1 out of 1 in 2e39

Go back to Iron Binding Sites List in 2e39
Iron binding site 1 out of 1 in the Crystal Structure of the Cn-Bound Form of Arthromyces Ramosus Peroxidase at 1.3 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of the Cn-Bound Form of Arthromyces Ramosus Peroxidase at 1.3 Angstroms Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:8.6
occ:1.00
 FE A:HEM401 0.0 8.6 1.0
C A:CYN503 1.9 9.1 1.0
NC A:HEM401 2.0 8.8 1.0
ND A:HEM401 2.0 7.4 1.0
NA A:HEM401 2.0 8.8 1.0
NB A:HEM401 2.0 8.5 1.0
NE2 A:HIS184 2.0 8.6 1.0
C4C A:HEM401 3.0 9.0 1.0
CE1 A:HIS184 3.0 9.2 1.0
C1D A:HEM401 3.0 8.8 1.0
C1C A:HEM401 3.0 8.0 1.0
C1A A:HEM401 3.0 7.3 1.0
C4A A:HEM401 3.1 9.3 1.0
C4D A:HEM401 3.1 7.3 1.0
C4B A:HEM401 3.1 8.5 1.0
N A:CYN503 3.1 12.2 1.0
CD2 A:HIS184 3.1 8.1 1.0
C1B A:HEM401 3.1 7.4 1.0
HE1 A:HIS184 3.2 11.0 1.0
HD2 A:HIS184 3.3 9.7 1.0
CHD A:HEM401 3.4 8.7 1.0
CHC A:HEM401 3.4 8.4 1.0
CHA A:HEM401 3.4 8.8 1.0
CHB A:HEM401 3.4 9.2 1.0
HG2 A:ARG52 4.1 10.7 1.0
ND1 A:HIS184 4.2 7.8 1.0
CG A:HIS184 4.2 8.0 1.0
C2C A:HEM401 4.3 8.2 1.0
C3D A:HEM401 4.3 7.3 1.0
C2D A:HEM401 4.3 7.5 1.0
C3C A:HEM401 4.3 8.0 1.0
C2A A:HEM401 4.3 7.8 1.0
C3A A:HEM401 4.3 8.4 1.0
C2B A:HEM401 4.3 7.6 1.0
C3B A:HEM401 4.3 8.6 1.0
HD2 A:PHE55 4.4 10.9 1.0
HE2 A:PHE55 4.6 13.1 1.0
O A:HOH1209 4.9 11.7 1.0

Reference:

K.Fukuyama, T.Okada. Structures of Cyanide, Nitric Oxide and Hydroxylamine Complexes of Arthromyces Ramosusperoxidase at 100 K Refined to 1.3 A Resolution: Coordination Geometries of the Ligands to the Haem Iron Acta Crystallogr.,Sect.D V. 63 472 2007.
ISSN: ISSN 0907-4449
PubMed: 17372351
DOI: 10.1107/S0907444907003812
Page generated: Sat Aug 3 20:59:37 2024

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