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Iron in PDB 1yzp: Substrate-Free Manganese Peroxidase

Enzymatic activity of Substrate-Free Manganese Peroxidase

All present enzymatic activity of Substrate-Free Manganese Peroxidase:
1.11.1.13;

Protein crystallography data

The structure of Substrate-Free Manganese Peroxidase, PDB code: 1yzp was solved by M.Sundaramoorthy, H.L.Youngs, M.H.Gold, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 1.60
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 160.595, 45.356, 52.817, 90.00, 97.25, 90.00
R / Rfree (%) 15.3 / 20.3

Other elements in 1yzp:

The structure of Substrate-Free Manganese Peroxidase also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Substrate-Free Manganese Peroxidase (pdb code 1yzp). 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 Substrate-Free Manganese Peroxidase, PDB code: 1yzp:

Iron binding site 1 out of 1 in 1yzp

Go back to Iron Binding Sites List in 1yzp
Iron binding site 1 out of 1 in the Substrate-Free Manganese Peroxidase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Substrate-Free Manganese Peroxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe396

b:18.4
occ:1.00
FE A:HEM396 0.0 18.4 1.0
O A:HOH1138 1.8 27.6 1.0
ND A:HEM396 2.0 17.3 1.0
NA A:HEM396 2.0 20.8 1.0
NB A:HEM396 2.0 16.2 1.0
NC A:HEM396 2.1 17.7 1.0
NE2 A:HIS173 2.1 14.4 1.0
C1D A:HEM396 3.0 13.2 1.0
C1B A:HEM396 3.0 19.8 1.0
C4D A:HEM396 3.0 18.9 1.0
C1A A:HEM396 3.0 22.0 1.0
C4A A:HEM396 3.0 16.8 1.0
C4C A:HEM396 3.1 17.8 1.0
CE1 A:HIS173 3.1 17.2 1.0
C4B A:HEM396 3.1 21.9 1.0
C1C A:HEM396 3.1 23.5 1.0
CD2 A:HIS173 3.2 17.3 1.0
CHB A:HEM396 3.4 20.8 1.0
CHA A:HEM396 3.4 18.0 1.0
CHD A:HEM396 3.4 15.7 1.0
CHC A:HEM396 3.5 19.3 1.0
O A:HOH1501 3.7 73.6 1.0
ND1 A:HIS173 4.2 17.9 1.0
C3D A:HEM396 4.2 18.4 1.0
C2D A:HEM396 4.2 14.2 1.0
C2A A:HEM396 4.3 18.0 1.0
C3A A:HEM396 4.3 19.1 1.0
CG A:HIS173 4.3 14.2 1.0
C2B A:HEM396 4.3 19.0 1.0
C3C A:HEM396 4.3 20.9 1.0
C2C A:HEM396 4.3 19.3 1.0
C3B A:HEM396 4.3 16.1 1.0
CG A:ARG42 4.5 9.8 0.5
NE A:ARG42 4.6 18.5 0.5
O A:HOH1410 4.8 91.4 1.0
CE2 A:PHE190 5.0 18.3 1.0
CD A:ARG42 5.0 14.3 0.5

Reference:

M.Sundaramoorthy, H.L.Youngs, M.H.Gold, T.L.Poulos. High-Resolution Crystal Structure of Manganese Peroxidase: Substrate and Inhibitor Complexes. Biochemistry V. 44 6463 2005.
ISSN: ISSN 0006-2960
PubMed: 15850380
DOI: 10.1021/BI047318E
Page generated: Sun Dec 13 14:38:27 2020

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