Atomistry » Iron » PDB 4a9v-4b2y » 4aul
Atomistry »
  Iron »
    PDB 4a9v-4b2y »
      4aul »

Iron in PDB 4aul: 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: 4aul 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) 28.96 / 1.50
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 200.958, 121.919, 124.919, 90.00, 115.28, 90.00
R / Rfree (%) 14.296 / 19.334

Other elements in 4aul:

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) 12 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 4aul). 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: 4aul:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 4aul

Go back to Iron Binding Sites List in 4aul
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:Fe754

b:10.1
occ:1.00
FE A:HEM754 0.0 10.1 1.0
OH A:TYR369 1.9 9.8 1.0
NC A:HEM754 2.0 8.9 1.0
NA A:HEM754 2.0 7.6 1.0
ND A:HEM754 2.1 8.4 1.0
NB A:HEM754 2.1 8.6 1.0
CZ A:TYR369 2.9 8.5 1.0
C4C A:HEM754 3.0 8.3 1.0
C4A A:HEM754 3.1 7.8 1.0
C1D A:HEM754 3.1 7.9 1.0
C1C A:HEM754 3.1 8.7 1.0
C4B A:HEM754 3.1 8.4 1.0
C1A A:HEM754 3.1 6.8 1.0
C4D A:HEM754 3.1 6.7 1.0
C1B A:HEM754 3.1 8.8 1.0
CHD A:HEM754 3.5 8.3 1.0
CHC A:HEM754 3.5 9.8 1.0
CHB A:HEM754 3.5 9.0 1.0
CHA A:HEM754 3.5 7.7 1.0
CE2 A:TYR369 3.6 8.4 1.0
O A:HOH2121 3.7 15.8 1.0
CE1 A:TYR369 3.9 10.0 1.0
NE A:ARG365 4.1 7.7 1.0
NH2 A:ARG365 4.2 7.5 1.0
C3A A:HEM754 4.3 6.8 1.0
C3C A:HEM754 4.3 7.7 1.0
C2A A:HEM754 4.3 6.8 1.0
C2C A:HEM754 4.4 7.9 1.0
C2D A:HEM754 4.4 8.5 1.0
C3B A:HEM754 4.4 8.3 1.0
C3D A:HEM754 4.4 7.0 1.0
C2B A:HEM754 4.4 9.1 1.0
CZ A:ARG365 4.5 7.6 1.0
CG2 A:VAL81 4.6 7.5 1.0
CZ A:PHE168 4.7 7.0 1.0
CD2 A:TYR369 4.9 7.8 1.0
CE2 A:PHE168 4.9 7.2 1.0

Iron binding site 2 out of 4 in 4aul

Go back to Iron Binding Sites List in 4aul
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:Fe754

b:10.5
occ:1.00
FE B:HEM754 0.0 10.5 1.0
NC B:HEM754 2.0 9.6 1.0
NA B:HEM754 2.0 9.2 1.0
OH B:TYR369 2.0 9.9 1.0
ND B:HEM754 2.1 8.0 1.0
NB B:HEM754 2.1 9.1 1.0
CZ B:TYR369 2.9 9.1 1.0
C1A B:HEM754 3.1 7.9 1.0
C4D B:HEM754 3.1 8.0 1.0
C4C B:HEM754 3.1 9.5 1.0
C1B B:HEM754 3.1 9.1 1.0
C1C B:HEM754 3.1 8.7 1.0
C1D B:HEM754 3.1 8.3 1.0
C4B B:HEM754 3.1 9.5 1.0
C4A B:HEM754 3.1 9.4 1.0
CHA B:HEM754 3.5 8.4 1.0
CHB B:HEM754 3.5 10.4 1.0
CHC B:HEM754 3.5 11.4 1.0
CHD B:HEM754 3.5 8.3 1.0
CE2 B:TYR369 3.6 8.1 1.0
O B:HOH2112 3.8 18.6 1.0
CE1 B:TYR369 3.9 10.7 1.0
NE B:ARG365 4.0 8.3 1.0
NH2 B:ARG365 4.1 8.1 1.0
C3C B:HEM754 4.3 9.8 1.0
C2A B:HEM754 4.4 8.9 1.0
C2C B:HEM754 4.4 9.7 1.0
C3D B:HEM754 4.4 7.2 1.0
C3A B:HEM754 4.4 8.1 1.0
C2B B:HEM754 4.4 8.1 1.0
C3B B:HEM754 4.4 9.0 1.0
C2D B:HEM754 4.4 9.2 1.0
CG2 B:VAL81 4.5 8.7 1.0
CZ B:ARG365 4.5 8.3 1.0
CZ B:PHE168 4.7 9.7 1.0
CD2 B:TYR369 4.8 8.2 1.0
CE2 B:PHE168 5.0 8.4 1.0

Iron binding site 3 out of 4 in 4aul

Go back to Iron Binding Sites List in 4aul
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:Fe754

b:10.3
occ:1.00
FE C:HEM754 0.0 10.3 1.0
OH C:TYR369 2.0 8.6 1.0
NC C:HEM754 2.0 9.0 1.0
NA C:HEM754 2.0 8.0 1.0
NB C:HEM754 2.0 7.9 1.0
ND C:HEM754 2.1 7.9 1.0
CZ C:TYR369 2.9 8.0 1.0
C1B C:HEM754 3.1 8.4 1.0
C4A C:HEM754 3.1 7.7 1.0
C1A C:HEM754 3.1 8.3 1.0
C4C C:HEM754 3.1 7.8 1.0
C4D C:HEM754 3.1 7.2 1.0
C1C C:HEM754 3.1 9.4 1.0
C4B C:HEM754 3.1 8.9 1.0
C1D C:HEM754 3.1 7.7 1.0
CHB C:HEM754 3.4 8.5 1.0
CHA C:HEM754 3.5 7.5 1.0
CHC C:HEM754 3.5 10.9 1.0
CHD C:HEM754 3.6 7.6 1.0
CE2 C:TYR369 3.6 8.7 1.0
O C:HOH2042 3.8 16.7 1.0
CE1 C:TYR369 3.9 9.5 1.0
NE C:ARG365 4.0 7.8 1.0
NH2 C:ARG365 4.1 7.5 1.0
C3A C:HEM754 4.3 7.9 1.0
C3C C:HEM754 4.3 7.7 1.0
C2A C:HEM754 4.4 8.1 1.0
C3B C:HEM754 4.4 9.3 1.0
C2B C:HEM754 4.4 7.8 1.0
C3D C:HEM754 4.4 7.0 1.0
C2D C:HEM754 4.4 7.6 1.0
C2C C:HEM754 4.4 8.8 1.0
CZ C:ARG365 4.5 7.6 1.0
CG2 C:VAL81 4.6 6.9 1.0
CZ C:PHE168 4.7 7.9 1.0
CD2 C:TYR369 4.9 8.0 1.0
CE2 C:PHE168 5.0 8.2 1.0

Iron binding site 4 out of 4 in 4aul

Go back to Iron Binding Sites List in 4aul
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:Fe754

b:10.4
occ:1.00
FE D:HEM754 0.0 10.4 1.0
NA D:HEM754 2.0 9.2 1.0
NC D:HEM754 2.0 8.1 1.0
OH D:TYR369 2.0 11.7 1.0
NB D:HEM754 2.1 9.2 1.0
ND D:HEM754 2.1 7.9 1.0
CZ D:TYR369 3.0 9.6 1.0
C4A D:HEM754 3.0 8.6 1.0
C1A D:HEM754 3.1 8.8 1.0
C1C D:HEM754 3.1 9.5 1.0
C1B D:HEM754 3.1 9.8 1.0
C4B D:HEM754 3.1 10.2 1.0
C4C D:HEM754 3.1 7.4 1.0
C4D D:HEM754 3.1 8.0 1.0
C1D D:HEM754 3.1 6.9 1.0
CHB D:HEM754 3.4 8.9 1.0
CHC D:HEM754 3.5 9.6 1.0
CHD D:HEM754 3.5 7.6 1.0
CHA D:HEM754 3.5 8.4 1.0
CE2 D:TYR369 3.6 9.5 1.0
O D:HOH2036 3.7 15.4 1.0
CE1 D:TYR369 3.9 10.1 1.0
NE D:ARG365 4.1 9.0 1.0
NH2 D:ARG365 4.2 8.0 1.0
C3A D:HEM754 4.3 7.4 1.0
C2A D:HEM754 4.3 7.3 1.0
C3C D:HEM754 4.4 8.0 1.0
C3B D:HEM754 4.4 11.3 1.0
C2C D:HEM754 4.4 7.9 1.0
C2B D:HEM754 4.4 8.2 1.0
C2D D:HEM754 4.4 7.0 1.0
C3D D:HEM754 4.4 7.4 1.0
CZ D:ARG365 4.5 8.2 1.0
CG2 D:VAL81 4.6 8.7 1.0
CZ D:PHE168 4.6 11.1 1.0
CD2 D:TYR369 4.9 9.4 1.0
CE2 D:PHE168 4.9 10.6 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 Dec 13 15:28:20 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy