Iron in PDB 2ghc: Conformational Mobility in the Active Site of A Heme Peroxidase

All present enzymatic activity of Conformational Mobility in the Active Site of A Heme Peroxidase:
1.11.1.11;

The structure of Conformational Mobility in the Active Site of A Heme Peroxidase, PDB code: 2ghc was solved by S.K.Badyal, M.G.Joyce, K.H.Sharp, E.L.Raven, P.C.Moody, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.64 / 1.25
Space group	P 42 21 2
Cell size a, b, c (Å), α, β, γ (°)	81.909, 81.909, 75.140, 90.00, 90.00, 90.00
R / Rfree (%)	18.9 / 20.7

The structure of Conformational Mobility in the Active Site of A Heme Peroxidase also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Iron atom in the Conformational Mobility in the Active Site of A Heme Peroxidase (pdb code 2ghc). 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 Conformational Mobility in the Active Site of A Heme Peroxidase, PDB code: 2ghc:

Iron binding site 1 out of 1 in the Conformational Mobility in the Active Site of A Heme Peroxidase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Conformational Mobility in the Active Site of A Heme Peroxidase within 5.0Å range: probe atom residue distance (Å) B Occ X:Fe251 b:5.3 occ:1.00 FE X:HEM251 0.0 5.3 1.0 N X:NO5503 1.8 3.4 0.5 N X:NO5503 1.8 16.5 0.5 NA X:HEM251 2.0 5.5 1.0 NC X:HEM251 2.0 5.5 1.0 NB X:HEM251 2.0 5.6 1.0 ND X:HEM251 2.0 5.5 1.0 NE2 X:HIS163 2.1 6.4 1.0 O X:NO5503 2.8 17.1 0.5 O X:NO5503 2.9 5.7 0.5 C1C X:HEM251 3.0 5.6 1.0 C1A X:HEM251 3.0 5.5 1.0 C4A X:HEM251 3.1 5.8 1.0 C4C X:HEM251 3.1 5.0 1.0 C4B X:HEM251 3.1 6.3 1.0 C1D X:HEM251 3.1 5.2 1.0 C4D X:HEM251 3.1 4.8 1.0 C1B X:HEM251 3.1 6.0 1.0 CD2 X:HIS163 3.1 6.2 1.0 CE1 X:HIS163 3.2 7.5 1.0 CHC X:HEM251 3.4 6.1 1.0 CHA X:HEM251 3.4 5.3 1.0 CHD X:HEM251 3.4 5.1 1.0 CHB X:HEM251 3.4 6.1 1.0 C2C X:HEM251 4.2 5.8 1.0 C3C X:HEM251 4.3 5.6 1.0 ND1 X:HIS163 4.3 6.9 1.0 C2A X:HEM251 4.3 5.7 1.0 CG X:HIS163 4.3 5.9 1.0 C2D X:HEM251 4.3 5.5 1.0 C3A X:HEM251 4.3 5.6 1.0 C3B X:HEM251 4.3 7.0 1.0 C2B X:HEM251 4.3 6.6 1.0 C3D X:HEM251 4.3 5.9 1.0 O X:HOH9357 4.3 23.2 1.0 O X:HOH9530 4.3 11.1 0.8 O X:HOH9533 4.4 32.3 1.0

S.K.Badyal, M.G.Joyce, K.H.Sharp, H.E.Seward, M.Mewies, J.Basran, I.K.Macdonald, P.C.E.Moody, E.L.Raven. Conformational Mobility in the Active Site of A Heme Peroxidase. J.Biol.Chem. V. 281 24512 2006.
ISSN: ISSN 0021-9258
PubMed: 16762924
DOI: 10.1074/JBC.M602602200