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Iron in PDB 1ly8: The Crystal Structure of A Mutant Enzyme of Coprinus Cinereus Peroxidase Provides An Understanding of Its Increased Thermostability and Insight Into Modelling of Protein Structures

Enzymatic activity of The Crystal Structure of A Mutant Enzyme of Coprinus Cinereus Peroxidase Provides An Understanding of Its Increased Thermostability and Insight Into Modelling of Protein Structures

All present enzymatic activity of The Crystal Structure of A Mutant Enzyme of Coprinus Cinereus Peroxidase Provides An Understanding of Its Increased Thermostability and Insight Into Modelling of Protein Structures:
1.11.1.7;

Protein crystallography data

The structure of The Crystal Structure of A Mutant Enzyme of Coprinus Cinereus Peroxidase Provides An Understanding of Its Increased Thermostability and Insight Into Modelling of Protein Structures, PDB code: 1ly8 was solved by K.Houborg, P.Harris, J.-C.N.Poulsen, A.Svendsen, P.Schneider, S.Larsen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.91 / 2.05
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 74.490, 114.860, 73.610, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / 24.9

Other elements in 1ly8:

The structure of The Crystal Structure of A Mutant Enzyme of Coprinus Cinereus Peroxidase Provides An Understanding of Its Increased Thermostability and Insight Into Modelling of Protein Structures also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Iron Binding Sites:

The binding sites of Iron atom in the The Crystal Structure of A Mutant Enzyme of Coprinus Cinereus Peroxidase Provides An Understanding of Its Increased Thermostability and Insight Into Modelling of Protein Structures (pdb code 1ly8). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the The Crystal Structure of A Mutant Enzyme of Coprinus Cinereus Peroxidase Provides An Understanding of Its Increased Thermostability and Insight Into Modelling of Protein Structures, PDB code: 1ly8:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1ly8

Go back to Iron Binding Sites List in 1ly8
Iron binding site 1 out of 2 in the The Crystal Structure of A Mutant Enzyme of Coprinus Cinereus Peroxidase Provides An Understanding of Its Increased Thermostability and Insight Into Modelling of Protein Structures


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Crystal Structure of A Mutant Enzyme of Coprinus Cinereus Peroxidase Provides An Understanding of Its Increased Thermostability and Insight Into Modelling of Protein Structures within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe344

b:9.9
occ:1.00
 FE A:HEM344 0.0 9.9 1.0
NB A:HEM344 2.0 9.8 1.0
NC A:HEM344 2.1 9.9 1.0
NA A:HEM344 2.1 9.8 1.0
ND A:HEM344 2.2 9.8 1.0
NE2 A:HIS183 2.2 10.5 1.0
C4B A:HEM344 3.0 10.2 1.0
C1A A:HEM344 3.0 9.6 1.0
C1C A:HEM344 3.0 10.3 1.0
C1B A:HEM344 3.1 9.8 1.0
C4D A:HEM344 3.1 9.6 1.0
C4C A:HEM344 3.1 9.9 1.0
C4A A:HEM344 3.2 9.6 1.0
CE1 A:HIS183 3.2 9.9 1.0
C1D A:HEM344 3.2 9.6 1.0
CD2 A:HIS183 3.2 9.9 1.0
CHC A:HEM344 3.3 9.9 1.0
CHA A:HEM344 3.3 9.7 1.0
CHB A:HEM344 3.4 9.7 1.0
CHD A:HEM344 3.4 9.6 1.0
O A:HOH9303 4.1 36.2 1.0
C2A A:HEM344 4.3 9.4 1.0
C3B A:HEM344 4.3 10.3 1.0
C2B A:HEM344 4.3 10.0 1.0
ND1 A:HIS183 4.3 9.3 1.0
C3A A:HEM344 4.4 9.4 1.0
CG A:HIS183 4.4 9.5 1.0
C3D A:HEM344 4.4 9.7 1.0
C2D A:HEM344 4.5 9.4 1.0
C2C A:HEM344 4.5 10.1 1.0
C3C A:HEM344 4.5 10.3 1.0
O A:HOH9094 4.8 25.9 1.0

Iron binding site 2 out of 2 in 1ly8

Go back to Iron Binding Sites List in 1ly8
Iron binding site 2 out of 2 in the The Crystal Structure of A Mutant Enzyme of Coprinus Cinereus Peroxidase Provides An Understanding of Its Increased Thermostability and Insight Into Modelling of Protein Structures


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of The Crystal Structure of A Mutant Enzyme of Coprinus Cinereus Peroxidase Provides An Understanding of Its Increased Thermostability and Insight Into Modelling of Protein Structures within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe344

b:11.1
occ:1.00
 FE B:HEM344 0.0 11.1 1.0
NA B:HEM344 2.0 10.5 1.0
NC B:HEM344 2.1 10.5 1.0
ND B:HEM344 2.1 10.2 1.0
NB B:HEM344 2.1 10.6 1.0
NE2 B:HIS183 2.3 9.6 1.0
C4D B:HEM344 3.0 9.8 1.0
C1A B:HEM344 3.0 10.4 1.0
C4A B:HEM344 3.0 10.6 1.0
C1B B:HEM344 3.1 10.9 1.0
C1D B:HEM344 3.1 10.1 1.0
C4C B:HEM344 3.1 10.6 1.0
C4B B:HEM344 3.2 11.3 1.0
C1C B:HEM344 3.2 10.8 1.0
CHA B:HEM344 3.2 9.9 1.0
CD2 B:HIS183 3.2 9.2 1.0
CE1 B:HIS183 3.3 9.9 1.0
CHB B:HEM344 3.4 10.6 1.0
CHD B:HEM344 3.4 10.0 1.0
CHC B:HEM344 3.4 10.9 1.0
O B:HOH9189 4.2 30.3 1.0
C2A B:HEM344 4.3 10.7 1.0
C3D B:HEM344 4.3 9.6 1.0
C2B B:HEM344 4.3 11.4 1.0
C2D B:HEM344 4.4 9.6 1.0
C3A B:HEM344 4.4 10.7 1.0
ND1 B:HIS183 4.4 9.3 1.0
C3B B:HEM344 4.4 11.9 1.0
CG B:HIS183 4.4 9.2 1.0
O B:HOH9089 4.5 19.7 1.0
C3C B:HEM344 4.6 10.6 1.0
C2C B:HEM344 4.6 10.5 1.0

Reference:

K.Houborg, P.Harris, J.C.Poulsen, P.Schneider, A.Svendsen, S.Larsen. The Structure of A Mutant Enzyme of Coprinus Cinereus Peroxidase Provides An Understanding of Its Increased Thermostability. Acta Crystallogr.,Sect.D V. 59 997 2003.
ISSN: ISSN 0907-4449
PubMed: 12777761
DOI: 10.1107/S0907444903006784
Page generated: Sat Aug 3 09:56:21 2024

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