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Iron in PDB 1dyt: X-Ray Crystal Structure of Ecp (Rnase 3) at 1.75 A

Protein crystallography data

The structure of X-Ray Crystal Structure of Ecp (Rnase 3) at 1.75 A, PDB code: 1dyt was solved by G.Mallorqui-Fernandez, J.Pous, R.Peracaula, T.Maeda, H.Tada, H.Yamada, M.Seno, R.De Llorens, F.X.Gomis-Rueth, M.Coll, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20 / 1.75
Space group P 43 2 2
Cell size a, b, c (Å), α, β, γ (°) 62.163, 62.163, 174.590, 90.00, 90.00, 90.00
R / Rfree (%) 22.4 / 27.1

Iron Binding Sites:

The binding sites of Iron atom in the X-Ray Crystal Structure of Ecp (Rnase 3) at 1.75 A (pdb code 1dyt). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the X-Ray Crystal Structure of Ecp (Rnase 3) at 1.75 A, PDB code: 1dyt:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1dyt

Go back to Iron Binding Sites List in 1dyt
Iron binding site 1 out of 2 in the X-Ray Crystal Structure of Ecp (Rnase 3) at 1.75 A


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of X-Ray Crystal Structure of Ecp (Rnase 3) at 1.75 A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe300

b:16.0
occ:0.50
O7 A:CIT302 2.3 44.0 0.5
O4 A:CIT302 2.3 30.4 0.5
C3 A:CIT302 3.1 44.8 0.5
C5 A:CIT302 3.2 37.4 0.5
C4 A:CIT302 3.5 36.9 0.5
O A:HOH2094 3.7 21.8 1.0
C2 A:CIT302 4.1 48.5 0.5
C6 A:CIT302 4.3 42.7 0.5
NH2 A:ARG34 4.4 18.4 1.0
O3 A:CIT302 4.4 32.8 0.5
O A:HOH2184 4.5 52.2 1.0
O5 A:CIT302 4.7 46.6 0.5
OD1 A:ASN39 4.7 16.1 0.5
CB A:ARG36 4.9 27.9 1.0
O A:HOH2140 5.0 31.4 1.0

Iron binding site 2 out of 2 in 1dyt

Go back to Iron Binding Sites List in 1dyt
Iron binding site 2 out of 2 in the X-Ray Crystal Structure of Ecp (Rnase 3) at 1.75 A


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of X-Ray Crystal Structure of Ecp (Rnase 3) at 1.75 A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe300

b:51.1
occ:0.50
O7 B:CIT302 3.5 39.7 0.5
O3 B:CIT302 3.5 39.8 0.5
C4 B:CIT302 3.6 33.4 0.5
C5 B:CIT302 3.8 38.5 0.5
O B:HOH2146 3.8 51.2 1.0
C3 B:CIT302 4.1 21.1 0.5
O B:HOH2068 4.8 30.8 1.0
O4 B:CIT302 4.8 46.4 0.5
O6 B:CIT302 4.9 25.4 0.5
C6 B:CIT302 4.9 32.6 0.5

Reference:

G.Mallorqui-Fernandez, J.Pous, R.Peracaula, T.Maeda, H.Tada, H.Yamada, M.Seno, R.De Llorens, F.X.Gomis-Rueth, M.Coll. Three-Dimensional Crystal Structure of Human Eosinophil Cationic Protein (Rnase 3) at 1.75 A Resolution. J.Mol.Biol. V. 300 1297 2000.
ISSN: ISSN 0022-2836
PubMed: 10903870
DOI: 10.1006/JMBI.2000.3939
Page generated: Sun Dec 13 14:11:45 2020

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