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Iron in PDB 4aue: Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum

Enzymatic activity of Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum

All present enzymatic activity of Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum:
1.11.1.6;

Protein crystallography data

The structure of Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum, PDB code: 4aue was solved by Y.Yuzugullu, C.H.Trinh, M.A.Smith, A.R.Pearson, S.E.V.Phillips, D.Sutay Kocabas, U.Bakir, Z.B.Ogel, M.J.Mcpherson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 141.42 / 2.70
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 185.447, 216.342, 68.607, 90.00, 90.00, 90.00
R / Rfree (%) 19.228 / 25.118

Other elements in 4aue:

The structure of Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum (pdb code 4aue). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum, PDB code: 4aue:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 4aue

Go back to Iron Binding Sites List in 4aue
Iron binding site 1 out of 4 in the Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe900

b:39.9
occ:1.00
 FE A:HDD900 0.0 39.9 1.0
OH A:TYR369 1.9 31.4 1.0
ND A:HDD900 1.9 38.2 1.0
NA A:HDD900 2.1 35.2 1.0
NC A:HDD900 2.1 35.9 1.0
NB A:HDD900 2.1 38.9 1.0
CZ A:TYR369 2.9 28.7 1.0
C4D A:HDD900 2.9 36.2 1.0
C1D A:HDD900 2.9 38.7 1.0
C1A A:HDD900 3.0 34.3 1.0
C4C A:HDD900 3.0 37.7 1.0
C4B A:HDD900 3.1 41.0 1.0
C4A A:HDD900 3.1 36.1 1.0
C1B A:HDD900 3.1 40.7 1.0
C1C A:HDD900 3.2 37.1 1.0
CHA A:HDD900 3.3 33.2 1.0
CHD A:HDD900 3.3 36.5 1.0
CHC A:HDD900 3.5 38.3 1.0
CHB A:HDD900 3.5 37.5 1.0
CE2 A:TYR369 3.6 28.8 1.0
CE1 A:TYR369 3.7 28.6 1.0
C3D A:HDD900 4.2 39.7 1.0
NE A:ARG365 4.2 31.8 1.0
C2D A:HDD900 4.3 40.0 1.0
NH2 A:ARG365 4.3 29.7 1.0
C2A A:HDD900 4.3 32.9 1.0
C3C A:HDD900 4.4 38.3 1.0
C3B A:HDD900 4.4 44.2 1.0
C3A A:HDD900 4.4 34.6 1.0
C2C A:HDD900 4.5 38.0 1.0
C2B A:HDD900 4.5 42.9 1.0
CG2 A:VAL81 4.5 30.5 1.0
CZ A:PHE168 4.5 29.3 1.0
CE1 A:HIS82 4.6 31.2 1.0
CZ A:ARG365 4.7 32.8 1.0
ND1 A:HIS82 4.7 35.2 1.0
CD2 A:TYR369 4.9 28.7 1.0
O1D A:HDD900 4.9 41.9 1.0
CD1 A:TYR369 5.0 29.5 1.0

Iron binding site 2 out of 4 in 4aue

Go back to Iron Binding Sites List in 4aue
Iron binding site 2 out of 4 in the Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe900

b:46.2
occ:1.00
 FE B:HDD900 0.0 46.2 1.0
ND B:HDD900 1.9 44.4 1.0
OH B:TYR369 2.0 33.3 1.0
NC B:HDD900 2.1 43.5 1.0
NA B:HDD900 2.1 45.5 1.0
NB B:HDD900 2.1 51.5 1.0
C4D B:HDD900 2.9 43.6 1.0
C1D B:HDD900 2.9 42.1 1.0
CZ B:TYR369 2.9 36.2 1.0
C4C B:HDD900 3.0 43.9 1.0
C1A B:HDD900 3.0 45.4 1.0
C1C B:HDD900 3.1 48.5 1.0
C4A B:HDD900 3.2 47.3 1.0
C4B B:HDD900 3.2 51.8 1.0
C1B B:HDD900 3.2 51.9 1.0
CHA B:HDD900 3.3 43.5 1.0
CHD B:HDD900 3.3 41.1 1.0
CHC B:HDD900 3.5 51.6 1.0
CHB B:HDD900 3.6 47.7 1.0
CE2 B:TYR369 3.6 35.9 1.0
CE1 B:TYR369 3.8 39.2 1.0
NE B:ARG365 4.2 43.6 1.0
C3D B:HDD900 4.2 48.5 1.0
C2D B:HDD900 4.3 47.8 1.0
NH2 B:ARG365 4.3 44.5 1.0
C3C B:HDD900 4.4 45.9 1.0
CG2 B:VAL81 4.4 34.1 1.0
C2A B:HDD900 4.4 44.7 1.0
C2C B:HDD900 4.4 44.0 1.0
C3A B:HDD900 4.5 47.5 1.0
C3B B:HDD900 4.5 55.4 1.0
C2B B:HDD900 4.5 57.3 1.0
CZ B:PHE168 4.5 39.1 1.0
CE1 B:HIS82 4.6 47.4 1.0
ND1 B:HIS82 4.7 49.0 1.0
CZ B:ARG365 4.7 44.5 1.0
CD2 B:TYR369 4.9 35.2 1.0
CD1 B:TYR369 5.0 40.8 1.0

Iron binding site 3 out of 4 in 4aue

Go back to Iron Binding Sites List in 4aue
Iron binding site 3 out of 4 in the Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe900

b:39.2
occ:1.00
 FE C:HDD900 0.0 39.2 1.0
OH C:TYR369 1.9 26.1 1.0
ND C:HDD900 1.9 38.9 1.0
NC C:HDD900 2.1 36.3 1.0
NA C:HDD900 2.1 39.8 1.0
NB C:HDD900 2.1 44.3 1.0
C1D C:HDD900 2.9 38.7 1.0
C4D C:HDD900 2.9 38.7 1.0
CZ C:TYR369 3.0 27.0 1.0
C4C C:HDD900 3.0 36.2 1.0
C1A C:HDD900 3.1 40.2 1.0
C1C C:HDD900 3.1 41.8 1.0
C1B C:HDD900 3.2 46.5 1.0
C4A C:HDD900 3.2 40.5 1.0
C4B C:HDD900 3.2 48.1 1.0
CHD C:HDD900 3.3 35.7 1.0
CHA C:HDD900 3.3 40.5 1.0
CHC C:HDD900 3.5 48.4 1.0
CHB C:HDD900 3.5 41.9 1.0
CE2 C:TYR369 3.7 27.6 1.0
CE1 C:TYR369 3.8 26.2 1.0
NE C:ARG365 4.1 34.1 1.0
C2D C:HDD900 4.2 39.7 1.0
C3D C:HDD900 4.3 40.8 1.0
C3C C:HDD900 4.3 39.8 1.0
NH2 C:ARG365 4.4 31.2 1.0
CZ C:PHE168 4.4 35.7 1.0
C2A C:HDD900 4.4 38.4 1.0
C2C C:HDD900 4.4 37.6 1.0
C3A C:HDD900 4.4 40.4 1.0
C3B C:HDD900 4.5 50.8 1.0
C2B C:HDD900 4.5 51.2 1.0
CG2 C:VAL81 4.5 29.5 1.0
CE1 C:HIS82 4.6 41.7 1.0
CZ C:ARG365 4.7 32.3 1.0
ND1 C:HIS82 4.8 41.6 1.0
CE2 C:PHE168 4.9 35.6 1.0
OND C:HDD900 5.0 38.5 1.0
CE1 C:PHE168 5.0 36.6 1.0

Iron binding site 4 out of 4 in 4aue

Go back to Iron Binding Sites List in 4aue
Iron binding site 4 out of 4 in the Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe900

b:37.2
occ:1.00
 FE D:HDD900 0.0 37.2 1.0
ND D:HDD900 1.9 37.8 1.0
OH D:TYR369 1.9 35.8 1.0
NC D:HDD900 2.1 37.0 1.0
NB D:HDD900 2.1 38.2 1.0
NA D:HDD900 2.1 36.1 1.0
CZ D:TYR369 2.9 39.4 1.0
C1D D:HDD900 2.9 39.7 1.0
C4D D:HDD900 2.9 40.0 1.0
C4C D:HDD900 3.0 36.1 1.0
C1A D:HDD900 3.1 36.3 1.0
C1B D:HDD900 3.1 39.5 1.0
C1C D:HDD900 3.1 38.1 1.0
C4B D:HDD900 3.1 39.4 1.0
C4A D:HDD900 3.2 35.7 1.0
CHD D:HDD900 3.3 38.5 1.0
CHA D:HDD900 3.3 38.5 1.0
CHB D:HDD900 3.5 37.2 1.0
CHC D:HDD900 3.5 38.7 1.0
CE2 D:TYR369 3.6 38.9 1.0
CE1 D:TYR369 3.8 40.3 1.0
NE D:ARG365 4.1 33.6 1.0
NH2 D:ARG365 4.2 30.1 1.0
C3D D:HDD900 4.2 39.7 1.0
C2D D:HDD900 4.2 40.8 1.0
C3C D:HDD900 4.4 36.2 1.0
C2A D:HDD900 4.4 38.4 1.0
C3B D:HDD900 4.4 38.6 1.0
C2C D:HDD900 4.4 35.9 1.0
C2B D:HDD900 4.5 40.7 1.0
C3A D:HDD900 4.5 36.7 1.0
CZ D:PHE168 4.5 41.4 1.0
CG2 D:VAL81 4.5 27.1 1.0
CE1 D:HIS82 4.6 36.1 1.0
CZ D:ARG365 4.6 33.2 1.0
ND1 D:HIS82 4.8 37.8 1.0
CD2 D:TYR369 4.9 40.7 1.0
O1D D:HDD900 4.9 44.1 1.0
CD1 D:TYR369 5.0 36.3 1.0

Reference:

Y.Yuzugullu, C.H.Trinh, M.A.Smith, A.R.Pearson, S.E.V.Phillips, D.Sutay Kocabas, U.Bakir, Z.B.Ogel, M.J.Mcpherson. Structure, Recombinant Expression and Mutagenesis Studies of the Catalase with Oxidase Activity From Scytalidium Thermophilum Acta Crystallogr.,Sect.D V. 69 398 2013.
ISSN: ISSN 0907-4449
PubMed: 23519415
DOI: 10.1107/S0907444912049001
Page generated: Sun Aug 4 23:45:45 2024

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