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Iron in PDB 4grc: Crystal Structure of Dyp-Type Peroxidase (SCO2276) From Streptomyces Coelicolor

Enzymatic activity of Crystal Structure of Dyp-Type Peroxidase (SCO2276) From Streptomyces Coelicolor

All present enzymatic activity of Crystal Structure of Dyp-Type Peroxidase (SCO2276) From Streptomyces Coelicolor:
1.11.1.19;

Protein crystallography data

The structure of Crystal Structure of Dyp-Type Peroxidase (SCO2276) From Streptomyces Coelicolor, PDB code: 4grc 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) 29.28 / 2.00
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 71.990, 71.990, 170.810, 90.00, 90.00, 120.00
R / Rfree (%) 15.9 / 19.8

Other elements in 4grc:

The structure of Crystal Structure of Dyp-Type Peroxidase (SCO2276) From Streptomyces Coelicolor also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Dyp-Type Peroxidase (SCO2276) From Streptomyces Coelicolor (pdb code 4grc). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Crystal Structure of Dyp-Type Peroxidase (SCO2276) From Streptomyces Coelicolor, PDB code: 4grc:

Iron binding site 1 out of 1 in 4grc

Go back to Iron Binding Sites List in 4grc
Iron binding site 1 out of 1 in the Crystal Structure of Dyp-Type Peroxidase (SCO2276) 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 (SCO2276) From Streptomyces Coelicolor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe502

b:18.5
occ:1.00
 FE A:HEM502 0.0 18.5 1.0
NB A:HEM502 2.0 20.1 1.0
NA A:HEM502 2.0 15.3 1.0
NC A:HEM502 2.0 15.8 1.0
ND A:HEM502 2.1 16.3 1.0
NE2 A:HIS326 2.3 18.9 1.0
O1 A:PEO503 2.8 38.2 1.0
C1C A:HEM502 3.1 16.2 1.0
C4B A:HEM502 3.1 17.9 1.0
C1A A:HEM502 3.1 16.3 1.0
C1B A:HEM502 3.1 17.6 1.0
C4D A:HEM502 3.1 16.6 1.0
C4A A:HEM502 3.1 20.3 1.0
C4C A:HEM502 3.1 17.0 1.0
C1D A:HEM502 3.1 15.8 1.0
CD2 A:HIS326 3.1 17.4 1.0
CE1 A:HIS326 3.3 19.7 1.0
CHC A:HEM502 3.4 18.2 1.0
CHA A:HEM502 3.4 16.8 1.0
CHB A:HEM502 3.5 16.6 1.0
CHD A:HEM502 3.5 15.4 1.0
O2 A:PEO503 3.8 32.0 1.0
NH1 A:ARG342 4.2 17.8 1.0
C2C A:HEM502 4.3 20.3 1.0
C2B A:HEM502 4.3 16.0 1.0
C3B A:HEM502 4.3 17.7 1.0
C2A A:HEM502 4.3 19.0 1.0
C3C A:HEM502 4.3 15.4 1.0
C3A A:HEM502 4.3 19.0 1.0
C3D A:HEM502 4.3 17.6 1.0
CG A:HIS326 4.3 18.6 1.0
C2D A:HEM502 4.3 17.4 1.0
ND1 A:HIS326 4.4 18.5 1.0
CD A:ARG342 4.6 19.9 1.0
CZ A:ARG342 4.9 22.9 1.0

Reference:

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.
Page generated: Tue Aug 5 10:45:58 2025

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