Iron in PDB 4aj9: Catalase 3 From Neurospora Crassa

All present enzymatic activity of Catalase 3 From Neurospora Crassa:
1.11.1.6;

The structure of Catalase 3 From Neurospora Crassa, PDB code: 4aj9 was solved by A.Zarate-Romero, E.Rudino-Pinera, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.70 / 1.85
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	130.750, 154.190, 160.300, 90.00, 90.00, 90.00
R / Rfree (%)	17.8 / 21.8

The binding sites of Iron atom in the Catalase 3 From Neurospora Crassa (pdb code 4aj9). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Catalase 3 From Neurospora Crassa, PDB code: 4aj9:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Catalase 3 From Neurospora Crassa


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Catalase 3 From Neurospora Crassa within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1715 b:3.8 occ:1.00 FE A:HEM1715 0.0 3.8 1.0 OH A:TYR389 2.0 5.7 1.0 NA A:HEM1715 2.0 2.0 1.0 NB A:HEM1715 2.1 2.3 1.0 NC A:HEM1715 2.1 2.8 1.0 ND A:HEM1715 2.1 3.0 1.0 CZ A:TYR389 3.0 3.8 1.0 C4A A:HEM1715 3.0 2.7 1.0 O A:HOH2105 3.0 13.2 1.0 C1B A:HEM1715 3.0 2.7 1.0 C1A A:HEM1715 3.1 3.3 1.0 C4B A:HEM1715 3.1 2.6 1.0 C4C A:HEM1715 3.1 1.8 1.0 C1D A:HEM1715 3.1 2.6 1.0 C4D A:HEM1715 3.1 5.5 1.0 C1C A:HEM1715 3.1 2.3 1.0 CHB A:HEM1715 3.4 3.6 1.0 CHD A:HEM1715 3.5 2.7 1.0 CHA A:HEM1715 3.5 2.2 1.0 CHC A:HEM1715 3.5 4.5 1.0 CE2 A:TYR389 3.8 2.9 1.0 CE1 A:TYR389 3.8 4.0 1.0 NE A:ARG385 4.2 1.7 1.0 O A:HOH2104 4.2 7.7 1.0 C3A A:HEM1715 4.2 4.0 1.0 C2B A:HEM1715 4.3 5.0 1.0 C2A A:HEM1715 4.3 3.2 1.0 C3B A:HEM1715 4.3 4.5 1.0 NH2 A:ARG385 4.3 1.8 1.0 C3C A:HEM1715 4.3 3.3 1.0 C2C A:HEM1715 4.3 2.4 1.0 C2D A:HEM1715 4.3 3.5 1.0 C3D A:HEM1715 4.3 2.0 1.0 CG2 A:VAL101 4.4 4.3 1.0 CZ A:PHE188 4.5 4.2 1.0 NE2 A:HIS102 4.6 3.6 1.0 CZ A:ARG385 4.7 8.8 1.0 CD2 A:HIS102 4.7 4.2 1.0

Iron binding site 2 out of 4 in the Catalase 3 From Neurospora Crassa


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Catalase 3 From Neurospora Crassa within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe1717 b:3.3 occ:1.00 FE B:HEM1717 0.0 3.3 1.0 OH B:TYR389 2.0 4.5 1.0 NC B:HEM1717 2.0 4.4 1.0 NA B:HEM1717 2.0 3.9 1.0 ND B:HEM1717 2.1 1.4 1.0 NB B:HEM1717 2.1 3.8 1.0 CZ B:TYR389 3.0 4.4 1.0 C4C B:HEM1717 3.0 4.3 1.0 C1A B:HEM1717 3.0 2.4 1.0 C1D B:HEM1717 3.1 2.2 1.0 C4B B:HEM1717 3.1 3.1 1.0 C1C B:HEM1717 3.1 2.5 1.0 C4D B:HEM1717 3.1 2.0 1.0 O B:HOH2073 3.1 9.2 1.0 C4A B:HEM1717 3.1 4.4 1.0 C1B B:HEM1717 3.1 4.4 1.0 CHD B:HEM1717 3.4 3.2 1.0 CHA B:HEM1717 3.4 1.7 1.0 CHC B:HEM1717 3.4 2.9 1.0 CHB B:HEM1717 3.4 2.1 1.0 CE1 B:TYR389 3.7 3.7 1.0 CE2 B:TYR389 3.9 4.2 1.0 NE B:ARG385 4.1 4.2 1.0 NH2 B:ARG385 4.1 4.2 1.0 O B:HOH2074 4.2 7.3 1.0 C3C B:HEM1717 4.2 2.0 1.0 C2C B:HEM1717 4.3 7.7 1.0 C2A B:HEM1717 4.3 4.0 1.0 C3B B:HEM1717 4.3 5.9 1.0 C2B B:HEM1717 4.3 2.6 1.0 C3A B:HEM1717 4.3 2.4 1.0 C3D B:HEM1717 4.3 1.2 1.0 C2D B:HEM1717 4.3 0.9 1.0 CG2 B:VAL101 4.5 2.4 1.0 CZ B:PHE188 4.6 6.8 1.0 CZ B:ARG385 4.6 4.4 1.0 NE2 B:HIS102 4.7 2.5 1.0 CD2 B:HIS102 4.8 3.1 1.0 CD1 B:TYR389 5.0 5.9 1.0

Iron binding site 3 out of 4 in the Catalase 3 From Neurospora Crassa


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Catalase 3 From Neurospora Crassa within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe1720 b:5.3 occ:1.00 FE C:HEM1720 0.0 5.3 1.0 OH C:TYR389 1.9 4.7 1.0 NA C:HEM1720 2.0 1.8 1.0 NB C:HEM1720 2.0 3.0 1.0 NC C:HEM1720 2.0 4.1 1.0 ND C:HEM1720 2.1 2.5 1.0 CZ C:TYR389 2.9 3.4 1.0 C1B C:HEM1720 3.0 3.6 1.0 C4A C:HEM1720 3.0 4.5 1.0 C1A C:HEM1720 3.1 3.3 1.0 C4B C:HEM1720 3.1 5.6 1.0 C4C C:HEM1720 3.1 5.4 1.0 C1C C:HEM1720 3.1 3.5 1.0 C4D C:HEM1720 3.1 1.6 1.0 C1D C:HEM1720 3.1 8.2 1.0 O C:HOH2053 3.4 18.7 1.0 CHB C:HEM1720 3.4 4.7 1.0 CHA C:HEM1720 3.4 3.4 1.0 CHC C:HEM1720 3.4 5.7 1.0 CHD C:HEM1720 3.5 5.9 1.0 CE1 C:TYR389 3.7 6.0 1.0 CE2 C:TYR389 3.8 4.6 1.0 NH2 C:ARG385 4.1 3.7 1.0 NE C:ARG385 4.2 3.7 1.0 O C:HOH2054 4.2 6.2 1.0 C2B C:HEM1720 4.2 4.4 1.0 C3A C:HEM1720 4.3 4.3 1.0 C3B C:HEM1720 4.3 3.6 1.0 C2A C:HEM1720 4.3 4.4 1.0 C3C C:HEM1720 4.3 8.3 1.0 C2C C:HEM1720 4.3 4.5 1.0 C3D C:HEM1720 4.3 1.0 1.0 C2D C:HEM1720 4.4 2.4 1.0 CZ C:PHE188 4.4 5.0 1.0 CG2 C:VAL101 4.4 2.0 1.0 CZ C:ARG385 4.5 3.3 1.0 NE2 C:HIS102 4.6 7.0 1.0 CD2 C:HIS102 4.7 2.2 1.0 CD1 C:TYR389 5.0 3.9 1.0 CE2 C:PHE188 5.0 4.6 1.0

Iron binding site 4 out of 4 in the Catalase 3 From Neurospora Crassa


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Catalase 3 From Neurospora Crassa within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe1716 b:4.7 occ:1.00 FE D:HEM1716 0.0 4.7 1.0 OH D:TYR389 1.9 3.4 1.0 NC D:HEM1716 2.0 1.9 1.0 NB D:HEM1716 2.0 5.5 1.0 NA D:HEM1716 2.1 4.8 1.0 ND D:HEM1716 2.1 4.6 1.0 CZ D:TYR389 3.0 2.6 1.0 O D:HOH2044 3.0 18.2 1.0 C4C D:HEM1716 3.0 5.6 1.0 C1B D:HEM1716 3.0 5.0 1.0 C4B D:HEM1716 3.0 3.1 1.0 C4A D:HEM1716 3.1 2.6 1.0 C1C D:HEM1716 3.1 4.3 1.0 C1D D:HEM1716 3.1 4.2 1.0 C1A D:HEM1716 3.1 2.2 1.0 C4D D:HEM1716 3.1 2.7 1.0 CHD D:HEM1716 3.4 4.7 1.0 CHB D:HEM1716 3.4 3.7 1.0 CHC D:HEM1716 3.4 5.3 1.0 CHA D:HEM1716 3.5 5.0 1.0 CE1 D:TYR389 3.7 1.6 1.0 CE2 D:TYR389 3.8 3.3 1.0 O D:HOH2045 4.1 7.0 1.0 NE D:ARG385 4.2 2.5 1.0 NH2 D:ARG385 4.2 1.6 1.0 C2B D:HEM1716 4.2 3.4 1.0 C3B D:HEM1716 4.2 3.0 1.0 C3C D:HEM1716 4.3 4.0 1.0 C2C D:HEM1716 4.3 3.7 1.0 C3A D:HEM1716 4.3 4.4 1.0 C2A D:HEM1716 4.3 3.0 1.0 C2D D:HEM1716 4.3 7.3 1.0 C3D D:HEM1716 4.4 4.2 1.0 CG2 D:VAL101 4.4 5.9 1.0 CZ D:PHE188 4.5 5.4 1.0 NE2 D:HIS102 4.6 6.5 1.0 CZ D:ARG385 4.6 4.0 1.0 CD2 D:HIS102 4.6 3.7 1.0 CD1 D:TYR389 5.0 6.4 1.0

A.Zarate-Romero, V.Stojanoff, A.E.Cohen, W.Hansberg, E.Rudino-Pinera. X-Ray Driven Reduction of Cpd I of Catalase-3 From N. Crassa Reveals Differential Sensitivity of Active Sites and Formation of Ferrous State. Arch.Biochem.Biophys. V. 666 107 2019.
ISSN: ESSN 1096-0384
PubMed: 30940570
DOI: 10.1016/J.ABB.2019.03.020