Iron in PDB 4gt2: Crystal Structure of Dyp-Type Peroxidase (SCO3963) From Streptomyces Coelicolor

All present enzymatic activity of Crystal Structure of Dyp-Type Peroxidase (SCO3963) From Streptomyces Coelicolor:
1.11.1.19;

The structure of Crystal Structure of Dyp-Type Peroxidase (SCO3963) From Streptomyces Coelicolor, PDB code: 4gt2 was solved by T.Lukk, A.M.A.Hetta, A.Jones, J.Solbiati, S.Majumdar, J.E.Cronan, J.A.Gerlt, S.K.Nair, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.20 / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	53.870, 203.200, 76.320, 90.00, 110.73, 90.00
R / Rfree (%)	14.7 / 18.5

The binding sites of Iron atom in the Crystal Structure of Dyp-Type Peroxidase (SCO3963) From Streptomyces Coelicolor (pdb code 4gt2). 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 of Dyp-Type Peroxidase (SCO3963) From Streptomyces Coelicolor, PDB code: 4gt2:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Crystal Structure of Dyp-Type Peroxidase (SCO3963) From Streptomyces Coelicolor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Dyp-Type Peroxidase (SCO3963) From Streptomyces Coelicolor within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:7.2 occ:1.00 FE B:HEM501 0.0 7.2 1.0 NB B:HEM501 2.0 8.3 1.0 NA B:HEM501 2.1 3.9 1.0 ND B:HEM501 2.1 6.3 1.0 NC B:HEM501 2.1 5.0 1.0 NE2 B:HIS353 2.3 7.7 1.0 O1 B:OXY503 2.8 26.8 1.0 C1B B:HEM501 3.1 9.0 1.0 C4B B:HEM501 3.1 8.2 1.0 C4A B:HEM501 3.1 8.6 1.0 C4D B:HEM501 3.1 8.5 1.0 C1A B:HEM501 3.1 7.2 1.0 C4C B:HEM501 3.1 7.9 1.0 C1D B:HEM501 3.1 6.3 1.0 C1C B:HEM501 3.1 6.6 1.0 CD2 B:HIS353 3.2 6.2 1.0 CE1 B:HIS353 3.3 8.0 1.0 CHB B:HEM501 3.4 9.4 1.0 CHA B:HEM501 3.5 9.1 1.0 CHC B:HEM501 3.5 7.4 1.0 CHD B:HEM501 3.5 7.3 1.0 O2 B:OXY503 4.0 29.0 1.0 NH1 B:ARG369 4.2 6.7 1.0 C2B B:HEM501 4.3 8.0 1.0 C3B B:HEM501 4.3 4.5 1.0 C3A B:HEM501 4.3 6.2 1.0 C2A B:HEM501 4.3 5.8 1.0 C3D B:HEM501 4.3 7.1 1.0 C3C B:HEM501 4.3 6.9 1.0 C2C B:HEM501 4.3 5.9 1.0 C2D B:HEM501 4.3 4.5 1.0 CG B:HIS353 4.3 6.9 1.0 ND1 B:HIS353 4.4 8.3 1.0 CD B:ARG369 4.5 8.1 1.0 CG2 B:THR357 4.9 4.4 1.0 CZ B:ARG369 4.9 7.0 1.0 NE B:ARG369 5.0 5.2 1.0

Iron binding site 2 out of 4 in the Crystal Structure of Dyp-Type Peroxidase (SCO3963) From Streptomyces Coelicolor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Dyp-Type Peroxidase (SCO3963) From Streptomyces Coelicolor within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:8.8 occ:1.00 FE A:HEM501 0.0 8.8 1.0 NA A:HEM501 2.1 6.5 1.0 NC A:HEM501 2.1 6.4 1.0 NB A:HEM501 2.1 8.3 1.0 ND A:HEM501 2.1 8.0 1.0 NE2 A:HIS353 2.3 10.6 1.0 O2 A:OXY503 2.8 28.6 1.0 C4A A:HEM501 3.1 8.3 1.0 C4C A:HEM501 3.1 6.3 1.0 C1D A:HEM501 3.1 9.0 1.0 C1B A:HEM501 3.1 7.0 1.0 C1A A:HEM501 3.1 9.7 1.0 C4D A:HEM501 3.1 8.0 1.0 C1C A:HEM501 3.1 9.9 1.0 C4B A:HEM501 3.1 12.5 1.0 CD2 A:HIS353 3.1 11.1 1.0 CE1 A:HIS353 3.3 8.1 1.0 CHD A:HEM501 3.4 9.8 1.0 CHB A:HEM501 3.4 5.9 1.0 CHA A:HEM501 3.5 8.5 1.0 CHC A:HEM501 3.5 13.0 1.0 O1 A:OXY503 3.9 27.8 1.0 NH1 A:ARG369 4.2 11.4 1.0 C3A A:HEM501 4.3 7.6 1.0 C3C A:HEM501 4.3 4.0 1.0 C2A A:HEM501 4.3 8.0 1.0 C2B A:HEM501 4.3 7.3 1.0 C2C A:HEM501 4.3 7.7 1.0 CG A:HIS353 4.3 11.1 1.0 C3D A:HEM501 4.3 6.6 1.0 C2D A:HEM501 4.3 7.1 1.0 C3B A:HEM501 4.3 7.9 1.0 CD A:ARG369 4.4 8.1 1.0 ND1 A:HIS353 4.4 11.8 1.0 CZ A:ARG369 4.8 9.0 1.0 NE A:ARG369 4.8 8.6 1.0 CG2 A:THR357 4.9 5.8 1.0

Iron binding site 3 out of 4 in the Crystal Structure of Dyp-Type Peroxidase (SCO3963) From Streptomyces Coelicolor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of Dyp-Type Peroxidase (SCO3963) From Streptomyces Coelicolor within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe501 b:10.1 occ:1.00 FE E:HEM501 0.0 10.1 1.0 NA E:HEM501 2.0 7.2 1.0 NC E:HEM501 2.1 5.9 1.0 NB E:HEM501 2.1 8.6 1.0 ND E:HEM501 2.1 8.9 1.0 NE2 E:HIS353 2.3 8.1 1.0 O1 E:OXY504 2.7 26.4 1.0 C4C E:HEM501 3.1 9.1 1.0 C1A E:HEM501 3.1 13.1 1.0 C4A E:HEM501 3.1 10.0 1.0 C1D E:HEM501 3.1 8.2 1.0 C1C E:HEM501 3.1 10.8 1.0 C4D E:HEM501 3.1 9.1 1.0 C4B E:HEM501 3.1 9.6 1.0 C1B E:HEM501 3.1 9.4 1.0 CD2 E:HIS353 3.2 8.9 1.0 CE1 E:HIS353 3.3 11.6 1.0 CHD E:HEM501 3.4 8.3 1.0 CHA E:HEM501 3.5 9.2 1.0 CHB E:HEM501 3.5 10.3 1.0 CHC E:HEM501 3.5 9.0 1.0 O2 E:OXY504 3.9 28.8 1.0 C2A E:HEM501 4.3 11.3 1.0 C3C E:HEM501 4.3 10.1 1.0 C3A E:HEM501 4.3 9.2 1.0 C2C E:HEM501 4.3 11.6 1.0 NH1 E:ARG369 4.3 12.2 1.0 C2D E:HEM501 4.3 8.2 1.0 C3B E:HEM501 4.3 9.0 1.0 C2B E:HEM501 4.3 8.4 1.0 CG E:HIS353 4.3 8.2 1.0 ND1 E:HIS353 4.3 10.9 1.0 C3D E:HEM501 4.3 6.7 1.0 CD E:ARG369 4.4 10.0 1.0 CZ E:ARG369 4.8 11.6 1.0 NE E:ARG369 4.9 9.9 1.0 CG2 E:THR357 4.9 12.0 1.0

Iron binding site 4 out of 4 in the Crystal Structure of Dyp-Type Peroxidase (SCO3963) From Streptomyces Coelicolor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of Dyp-Type Peroxidase (SCO3963) From Streptomyces Coelicolor within 5.0Å range: probe atom residue distance (Å) B Occ G:Fe501 b:8.7 occ:1.00 FE G:HEM501 0.0 8.7 1.0 NC G:HEM501 2.0 8.0 1.0 ND G:HEM501 2.1 4.8 1.0 NA G:HEM501 2.1 6.4 1.0 NB G:HEM501 2.1 11.3 1.0 NE2 G:HIS353 2.3 5.6 1.0 O2 G:OXY502 2.8 21.3 1.0 C4C G:HEM501 3.0 6.8 1.0 C1C G:HEM501 3.1 6.2 1.0 C1D G:HEM501 3.1 6.2 1.0 C4D G:HEM501 3.1 7.2 1.0 C1A G:HEM501 3.1 8.9 1.0 C4A G:HEM501 3.1 4.8 1.0 C1B G:HEM501 3.1 8.6 1.0 C4B G:HEM501 3.1 7.5 1.0 CD2 G:HIS353 3.2 8.3 1.0 CE1 G:HIS353 3.2 5.6 1.0 CHD G:HEM501 3.4 7.3 1.0 CHA G:HEM501 3.4 7.0 1.0 CHB G:HEM501 3.5 7.5 1.0 CHC G:HEM501 3.5 6.9 1.0 O1 G:OXY502 4.0 23.6 1.0 C3C G:HEM501 4.3 7.1 1.0 C2C G:HEM501 4.3 4.0 1.0 C3A G:HEM501 4.3 8.0 1.0 C2A G:HEM501 4.3 6.3 1.0 C3D G:HEM501 4.3 5.2 1.0 NH1 G:ARG369 4.3 9.5 1.0 C2D G:HEM501 4.3 5.9 1.0 ND1 G:HIS353 4.3 8.8 1.0 CG G:HIS353 4.3 9.3 1.0 C2B G:HEM501 4.4 8.5 1.0 C3B G:HEM501 4.4 5.9 1.0 CD G:ARG369 4.5 9.6 1.0 CG2 G:THR357 4.8 7.1 1.0 CZ G:ARG369 4.9 8.7 1.0 NE G:ARG369 5.0 9.8 1.0 CE1 G:PHE390 5.0 12.4 1.0

T.Lukk, A.M.A.Hetta, A.Jones, J.Solbiati, S.Majumdar, J.E.Cronan, J.A.Gerlt, S.K.Nair. Dyp-Type Peroxidases From Stretptomyces and Thermobifida Can Modify Organosolv Lignin. To Be Published.