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 Aug 4 23:45:46 2024

Last articles

F in 5G48
F in 5G4M
F in 5G1A
F in 5G11
F in 5G3J
F in 5G17
F in 5G10
F in 5FWG
F in 5G0T
F in 5G0U
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy