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Iron in PDB 4aum: 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: 4aum 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) 113.00 / 1.40
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 201.420, 121.447, 125.208, 90.00, 115.51, 90.00
R / Rfree (%) 11.812 / 14.55

Other elements in 4aum:

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) 10 atoms

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 4aum). 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: 4aum:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 4aum

Go back to Iron Binding Sites List in 4aum
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:7.6
occ:1.00
FE A:HDD900 0.0 7.6 1.0
ND A:HDD900 2.0 7.2 1.0
OH A:TYR369 2.0 7.3 1.0
NA A:HDD900 2.0 6.4 1.0
NC A:HDD900 2.1 6.7 1.0
NB A:HDD900 2.1 7.0 1.0
O A:HOH2119 2.3 10.9 0.3
CZ A:TYR369 3.0 6.2 1.0
C1D A:HDD900 3.0 6.6 1.0
C4A A:HDD900 3.0 6.4 1.0
C4D A:HDD900 3.0 6.2 1.0
C1A A:HDD900 3.1 6.1 1.0
C4C A:HDD900 3.1 6.7 1.0
C1B A:HDD900 3.1 7.4 1.0
C4B A:HDD900 3.1 7.0 1.0
C1C A:HDD900 3.1 6.7 1.0
CHA A:HDD900 3.4 6.1 1.0
CHB A:HDD900 3.4 7.0 1.0
CHD A:HDD900 3.4 6.5 1.0
CHC A:HDD900 3.5 7.3 1.0
CE2 A:TYR369 3.7 5.3 1.0
CE1 A:TYR369 3.8 7.1 1.0
NE A:ARG365 4.1 6.2 1.0
NH2 A:ARG365 4.2 6.5 1.0
O A:HOH2118 4.2 16.3 1.0
C2A A:HDD900 4.3 5.5 1.0
C3B A:HDD900 4.3 7.8 1.0
C3A A:HDD900 4.3 6.1 1.0
C3C A:HDD900 4.3 7.2 1.0
C2B A:HDD900 4.4 7.2 1.0
C2C A:HDD900 4.4 7.5 1.0
C2D A:HDD900 4.4 7.7 1.0
C3D A:HDD900 4.4 7.4 1.0
CZ A:ARG365 4.6 6.3 1.0
CG2 A:VAL81 4.6 6.9 1.0
CZ A:PHE168 4.6 9.0 1.0
NE2 A:HIS82 4.8 7.4 1.0
CD2 A:HIS82 4.8 6.3 1.0
CE2 A:PHE168 4.9 8.4 1.0
CD2 A:TYR369 5.0 6.8 1.0

Iron binding site 2 out of 4 in 4aum

Go back to Iron Binding Sites List in 4aum
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:8.3
occ:1.00
FE B:HDD900 0.0 8.3 1.0
OH B:TYR369 2.0 8.2 1.0
ND B:HDD900 2.0 7.0 1.0
NA B:HDD900 2.0 7.2 1.0
NC B:HDD900 2.1 7.5 1.0
NB B:HDD900 2.1 7.5 1.0
O B:HOH2112 2.3 11.5 0.3
CZ B:TYR369 3.0 6.8 1.0
C4D B:HDD900 3.0 6.6 1.0
C1D B:HDD900 3.0 6.6 1.0
C4A B:HDD900 3.0 7.4 1.0
C4C B:HDD900 3.0 7.5 1.0
C1A B:HDD900 3.1 6.1 1.0
C1B B:HDD900 3.1 8.3 1.0
C4B B:HDD900 3.1 7.3 1.0
C1C B:HDD900 3.1 6.8 1.0
CHA B:HDD900 3.4 6.5 1.0
CHD B:HDD900 3.4 7.5 1.0
CHB B:HDD900 3.4 8.3 1.0
CHC B:HDD900 3.5 7.2 1.0
CE2 B:TYR369 3.7 6.4 1.0
CE1 B:TYR369 3.8 8.2 1.0
NE B:ARG365 4.1 6.8 1.0
NH2 B:ARG365 4.2 7.3 1.0
C2A B:HDD900 4.3 6.8 1.0
C3C B:HDD900 4.3 7.8 1.0
C3A B:HDD900 4.3 6.7 1.0
C3B B:HDD900 4.3 8.1 1.0
C2C B:HDD900 4.4 7.5 1.0
C2B B:HDD900 4.4 8.2 1.0
C3D B:HDD900 4.4 7.4 1.0
C2D B:HDD900 4.4 8.1 1.0
O B:HOH2111 4.5 16.8 1.0
CG2 B:VAL81 4.6 7.3 1.0
CZ B:ARG365 4.6 6.6 1.0
CZ B:PHE168 4.7 10.1 1.0
NE2 B:HIS82 4.8 8.0 1.0
CD2 B:HIS82 4.8 7.3 1.0
CE2 B:PHE168 4.9 9.8 1.0
CD2 B:TYR369 5.0 6.8 1.0

Iron binding site 3 out of 4 in 4aum

Go back to Iron Binding Sites List in 4aum
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:7.4
occ:1.00
FE C:HDD900 0.0 7.4 1.0
OH C:TYR369 2.0 7.7 1.0
ND C:HDD900 2.0 6.3 1.0
NA C:HDD900 2.0 6.5 1.0
NB C:HDD900 2.1 6.8 1.0
NC C:HDD900 2.1 6.4 1.0
O C:HOH2042 2.3 9.8 0.3
CZ C:TYR369 3.0 6.3 1.0
C4A C:HDD900 3.0 6.8 1.0
C1A C:HDD900 3.0 5.7 1.0
C1D C:HDD900 3.1 6.0 1.0
C4C C:HDD900 3.1 5.9 1.0
C4D C:HDD900 3.1 6.2 1.0
C1B C:HDD900 3.1 7.2 1.0
C4B C:HDD900 3.1 7.1 1.0
C1C C:HDD900 3.1 6.5 1.0
CHA C:HDD900 3.4 6.0 1.0
CHD C:HDD900 3.4 6.6 1.0
CHB C:HDD900 3.4 7.7 1.0
CHC C:HDD900 3.4 6.8 1.0
CE2 C:TYR369 3.7 6.3 1.0
CE1 C:TYR369 3.8 7.3 1.0
O C:HOH2041 3.9 19.5 1.0
NE C:ARG365 4.1 6.2 1.0
NH2 C:ARG365 4.2 7.0 1.0
C2A C:HDD900 4.3 5.8 1.0
C3A C:HDD900 4.3 6.2 1.0
C3B C:HDD900 4.3 7.8 1.0
C3C C:HDD900 4.3 6.6 1.0
C2B C:HDD900 4.4 7.2 1.0
C2C C:HDD900 4.4 6.9 1.0
C3D C:HDD900 4.4 7.0 1.0
C2D C:HDD900 4.4 6.9 1.0
CG2 C:VAL81 4.6 7.2 1.0
CZ C:ARG365 4.6 6.4 1.0
CZ C:PHE168 4.7 8.2 1.0
NE2 C:HIS82 4.8 7.6 1.0
CD2 C:HIS82 4.8 6.9 1.0
CE2 C:PHE168 4.9 7.9 1.0
CD2 C:TYR369 5.0 6.8 1.0

Iron binding site 4 out of 4 in 4aum

Go back to Iron Binding Sites List in 4aum
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:8.0
occ:1.00
FE D:HDD900 0.0 8.0 1.0
OH D:TYR369 2.0 7.4 1.0
ND D:HDD900 2.0 7.2 1.0
NA D:HDD900 2.0 7.3 1.0
NC D:HDD900 2.1 6.9 1.0
NB D:HDD900 2.1 7.8 1.0
O D:HOH2039 2.3 11.6 0.3
CZ D:TYR369 3.0 6.7 1.0
C4D D:HDD900 3.0 6.5 1.0
C1A D:HDD900 3.0 6.8 1.0
C4A D:HDD900 3.0 7.2 1.0
C1D D:HDD900 3.0 7.1 1.0
C4C D:HDD900 3.1 7.3 1.0
C4B D:HDD900 3.1 7.9 1.0
C1B D:HDD900 3.1 7.8 1.0
C1C D:HDD900 3.1 6.8 1.0
CHA D:HDD900 3.4 7.0 1.0
CHD D:HDD900 3.4 7.3 1.0
CHB D:HDD900 3.4 8.7 1.0
CHC D:HDD900 3.5 8.1 1.0
CE2 D:TYR369 3.7 7.1 1.0
CE1 D:TYR369 3.8 7.6 1.0
O D:HOH2040 4.0 20.1 1.0
NE D:ARG365 4.1 6.5 1.0
NH2 D:ARG365 4.2 6.7 1.0
C2A D:HDD900 4.3 6.7 1.0
C3B D:HDD900 4.3 8.4 1.0
C3A D:HDD900 4.3 6.5 1.0
C3C D:HDD900 4.4 7.8 1.0
C2C D:HDD900 4.4 7.2 1.0
C2B D:HDD900 4.4 7.3 1.0
C3D D:HDD900 4.4 7.5 1.0
C2D D:HDD900 4.4 8.0 1.0
CG2 D:VAL81 4.6 7.7 1.0
CZ D:ARG365 4.6 6.8 1.0
CZ D:PHE168 4.7 10.1 1.0
NE2 D:HIS82 4.8 8.3 1.0
CD2 D:HIS82 4.8 7.3 1.0
CE2 D:PHE168 4.9 9.6 1.0
CD2 D:TYR369 5.0 6.6 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 23:45:49 2024

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