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Iron in PDB 2w23: Structure of Mutant W169Y of Pleurotus Eryngii Versatile Peroxidase (Vp)

Enzymatic activity of Structure of Mutant W169Y of Pleurotus Eryngii Versatile Peroxidase (Vp)

All present enzymatic activity of Structure of Mutant W169Y of Pleurotus Eryngii Versatile Peroxidase (Vp):
1.11.1.16;

Protein crystallography data

The structure of Structure of Mutant W169Y of Pleurotus Eryngii Versatile Peroxidase (Vp), PDB code: 2w23 was solved by F.J.Ruiz-Duenas, R.Pogni, M.Morales, S.Giansanti, M.J.Mate, A.Romero, M.J.Martinez, R.Basosi, A.T.Martinez, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 31.01 / 1.94
Space group I 41
Cell size a, b, c (Å), α, β, γ (°) 96.740, 96.740, 98.190, 90.00, 90.00, 90.00
R / Rfree (%) 14.2 / 17.5

Other elements in 2w23:

The structure of Structure of Mutant W169Y of Pleurotus Eryngii Versatile Peroxidase (Vp) also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Mutant W169Y of Pleurotus Eryngii Versatile Peroxidase (Vp) (pdb code 2w23). 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 Structure of Mutant W169Y of Pleurotus Eryngii Versatile Peroxidase (Vp), PDB code: 2w23:

Iron binding site 1 out of 1 in 2w23

Go back to Iron Binding Sites List in 2w23
Iron binding site 1 out of 1 in the Structure of Mutant W169Y of Pleurotus Eryngii Versatile Peroxidase (Vp)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Mutant W169Y of Pleurotus Eryngii Versatile Peroxidase (Vp) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1316

b:8.2
occ:1.00
 FE A:HEM1316 0.0 8.2 1.0
NA A:HEM1316 2.1 6.5 1.0
NB A:HEM1316 2.1 8.3 1.0
NC A:HEM1316 2.1 8.1 1.0
ND A:HEM1316 2.1 7.8 1.0
NE2 A:HIS169 2.2 6.6 1.0
O A:HOH2059 2.8 25.5 1.0
C4A A:HEM1316 3.1 9.2 1.0
C1D A:HEM1316 3.1 7.5 1.0
C1B A:HEM1316 3.1 7.7 1.0
C1A A:HEM1316 3.1 8.2 1.0
C4B A:HEM1316 3.1 9.0 1.0
C4C A:HEM1316 3.1 7.9 1.0
C1C A:HEM1316 3.1 7.6 1.0
C4D A:HEM1316 3.1 8.1 1.0
CE1 A:HIS169 3.1 6.4 1.0
CD2 A:HIS169 3.2 6.1 1.0
CHB A:HEM1316 3.4 8.1 1.0
CHD A:HEM1316 3.5 5.8 1.0
CHC A:HEM1316 3.5 6.0 1.0
CHA A:HEM1316 3.5 6.1 1.0
ND1 A:HIS169 4.3 5.7 1.0
C2D A:HEM1316 4.3 6.7 1.0
C3D A:HEM1316 4.3 7.7 1.0
C2B A:HEM1316 4.3 8.5 1.0
C2A A:HEM1316 4.3 8.3 1.0
C3A A:HEM1316 4.3 7.8 1.0
C3B A:HEM1316 4.3 9.6 1.0
CG A:HIS169 4.3 5.5 1.0
C2C A:HEM1316 4.3 8.5 1.0
C3C A:HEM1316 4.3 7.4 1.0
O A:HOH2169 4.7 40.0 1.0
CE2 A:PHE186 4.9 6.5 1.0
CD2 A:LEU166 5.0 5.6 1.0

Reference:

F.J.Ruiz-Duenas, R.Pogni, M.Morales, S.Giansanti, M.J.Mate, A.Romero, M.J.Martinez, R.Basosi, A.T.Martinez. Protein Radicals in Fungal Versatile Peroxidase: Catalytic Tryptophan Radical in Both Compound I and Compound II and Studies on W164Y, W164H, and W164S Variants. J.Biol.Chem. V. 284 7986 2009.
ISSN: ISSN 0021-9258
PubMed: 19158088
DOI: 10.1074/JBC.M808069200
Page generated: Sun Aug 4 03:18:42 2024

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