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Iron in PDB 1dii: Crystal Structure of P-Cresol Methylhydroxylase at 2.5 A Resolution

Enzymatic activity of Crystal Structure of P-Cresol Methylhydroxylase at 2.5 A Resolution

All present enzymatic activity of Crystal Structure of P-Cresol Methylhydroxylase at 2.5 A Resolution:
1.17.99.1;

Protein crystallography data

The structure of Crystal Structure of P-Cresol Methylhydroxylase at 2.5 A Resolution, PDB code: 1dii was solved by L.M.Cunane, Z.W.Chen, N.Shamala, F.S.Mathews, C.N.Cronin, W.S.Mcintire, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 140.300, 130.600, 74.100, 90.00, 90.00, 90.00
R / Rfree (%) 17.2 / 23

Other elements in 1dii:

The structure of Crystal Structure of P-Cresol Methylhydroxylase at 2.5 A Resolution also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of P-Cresol Methylhydroxylase at 2.5 A Resolution (pdb code 1dii). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of P-Cresol Methylhydroxylase at 2.5 A Resolution, PDB code: 1dii:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1dii

Go back to Iron Binding Sites List in 1dii
Iron binding site 1 out of 2 in the Crystal Structure of P-Cresol Methylhydroxylase at 2.5 A Resolution


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 P-Cresol Methylhydroxylase at 2.5 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe699

b:30.4
occ:1.00
FE C:HEM699 0.0 30.4 1.0
ND C:HEM699 2.0 32.0 1.0
NC C:HEM699 2.0 37.6 1.0
NA C:HEM699 2.0 41.4 1.0
NB C:HEM699 2.0 33.1 1.0
NE2 C:HIS619 2.0 17.3 1.0
SD C:MET650 2.3 30.3 1.0
CE1 C:HIS619 3.0 17.7 1.0
C1A C:HEM699 3.0 47.0 1.0
C1D C:HEM699 3.0 24.7 1.0
C4D C:HEM699 3.0 36.1 1.0
C4C C:HEM699 3.0 33.5 1.0
C1B C:HEM699 3.1 39.5 1.0
C4A C:HEM699 3.1 43.3 1.0
C1C C:HEM699 3.1 35.4 1.0
C4B C:HEM699 3.1 33.4 1.0
CD2 C:HIS619 3.1 15.0 1.0
CHD C:HEM699 3.4 29.9 1.0
CG C:MET650 3.4 32.5 1.0
CHA C:HEM699 3.4 31.2 1.0
CE C:MET650 3.4 18.9 1.0
CHB C:HEM699 3.4 44.9 1.0
CHC C:HEM699 3.5 36.5 1.0
CG C:HIS619 4.1 27.0 1.0
ND1 C:HIS619 4.2 29.2 1.0
C2D C:HEM699 4.3 31.8 1.0
C3D C:HEM699 4.3 37.8 1.0
C3C C:HEM699 4.3 33.4 1.0
CB C:MET650 4.3 35.2 1.0
C2A C:HEM699 4.3 43.3 1.0
C3A C:HEM699 4.3 38.4 1.0
C2B C:HEM699 4.3 38.7 1.0
C3B C:HEM699 4.3 33.1 1.0
C2C C:HEM699 4.3 23.5 1.0

Iron binding site 2 out of 2 in 1dii

Go back to Iron Binding Sites List in 1dii
Iron binding site 2 out of 2 in the Crystal Structure of P-Cresol Methylhydroxylase at 2.5 A Resolution


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 P-Cresol Methylhydroxylase at 2.5 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe699

b:35.9
occ:1.00
FE D:HEM699 0.0 35.9 1.0
ND D:HEM699 2.0 42.0 1.0
NC D:HEM699 2.0 41.8 1.0
NB D:HEM699 2.0 38.2 1.0
NA D:HEM699 2.0 51.5 1.0
NE2 D:HIS619 2.1 25.7 1.0
SD D:MET650 2.2 27.1 1.0
CE1 D:HIS619 3.0 27.0 1.0
C1D D:HEM699 3.0 45.3 1.0
C4D D:HEM699 3.0 45.4 1.0
C1C D:HEM699 3.0 41.4 1.0
C1B D:HEM699 3.0 48.2 1.0
C4C D:HEM699 3.0 40.0 1.0
C1A D:HEM699 3.1 57.5 1.0
C4B D:HEM699 3.1 41.4 1.0
C4A D:HEM699 3.1 52.2 1.0
CD2 D:HIS619 3.2 26.0 1.0
CHD D:HEM699 3.4 45.2 1.0
CG D:MET650 3.4 33.8 1.0
CHB D:HEM699 3.4 52.7 1.0
CHA D:HEM699 3.4 54.4 1.0
CHC D:HEM699 3.4 41.3 1.0
CE D:MET650 3.4 28.1 1.0
CG D:HIS619 4.2 31.6 1.0
ND1 D:HIS619 4.2 33.1 1.0
C2D D:HEM699 4.3 50.0 1.0
C3D D:HEM699 4.3 45.3 1.0
CB D:MET650 4.3 34.1 1.0
C3C D:HEM699 4.3 33.1 1.0
C2B D:HEM699 4.3 50.5 1.0
C3B D:HEM699 4.3 45.4 1.0
C2C D:HEM699 4.3 41.3 1.0
C2A D:HEM699 4.3 55.4 1.0
C3A D:HEM699 4.3 54.4 1.0

Reference:

L.M.Cunane, Z.W.Chen, N.Shamala, F.S.Mathews, C.N.Cronin, W.S.Mcintire. Structures of the Flavocytochrome P-Cresol Methylhydroxylase and Its Enzyme-Substrate Complex: Gated Substrate Entry and Proton Relays Support the Proposed Catalytic Mechanism. J.Mol.Biol. V. 295 357 2000.
ISSN: ISSN 0022-2836
PubMed: 10623531
DOI: 10.1006/JMBI.1999.3290
Page generated: Sun Dec 13 14:10:27 2020

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