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Iron in PDB 1e5s: Proline 3-Hydroxylase (Type II) - Iron Form

Protein crystallography data

The structure of Proline 3-Hydroxylase (Type II) - Iron Form, PDB code: 1e5s was solved by I.J.Clifton, L.C.Hsueh, J.E.Baldwin, C.J.Schofield, K.Harlos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 23.82 / 2.40
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 72.780, 72.780, 224.900, 90.00, 90.00, 120.00
R / Rfree (%) 21.6 / 27.1

Iron Binding Sites:

The binding sites of Iron atom in the Proline 3-Hydroxylase (Type II) - Iron Form (pdb code 1e5s). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Proline 3-Hydroxylase (Type II) - Iron Form, PDB code: 1e5s:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1e5s

Go back to Iron Binding Sites List in 1e5s
Iron binding site 1 out of 2 in the Proline 3-Hydroxylase (Type II) - Iron Form


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Proline 3-Hydroxylase (Type II) - Iron Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe800

b:62.1
occ:1.00
NE2 A:HIS158 2.3 49.9 1.0
OD1 A:ASP109 2.3 58.4 1.0
NE2 A:HIS107 2.4 34.5 1.0
CE1 A:HIS107 2.9 42.8 1.0
OD2 A:ASP109 3.0 53.3 1.0
CG A:ASP109 3.1 54.8 1.0
CE1 A:HIS158 3.2 49.0 1.0
CD2 A:HIS158 3.3 47.6 1.0
CD2 A:HIS107 3.6 39.7 1.0
ND1 A:HIS107 4.2 38.3 1.0
ND1 A:HIS158 4.3 49.8 1.0
O A:HOH2114 4.3 72.1 1.0
CG A:HIS158 4.4 48.2 1.0
CG A:HIS107 4.5 39.4 1.0
CB A:ASP109 4.5 55.0 1.0
O A:HOH2035 4.9 73.9 1.0
O A:HIS107 5.0 36.2 1.0

Iron binding site 2 out of 2 in 1e5s

Go back to Iron Binding Sites List in 1e5s
Iron binding site 2 out of 2 in the Proline 3-Hydroxylase (Type II) - Iron Form


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Proline 3-Hydroxylase (Type II) - Iron Form within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe801

b:60.1
occ:1.00
NE2 B:HIS158 2.1 54.1 1.0
NE2 B:HIS107 2.2 51.2 1.0
OD1 B:ASP109 2.3 68.7 1.0
OD2 B:ASP109 2.9 74.2 1.0
CG B:ASP109 2.9 66.6 1.0
CE1 B:HIS158 3.0 53.3 1.0
CE1 B:HIS107 3.1 53.1 1.0
CD2 B:HIS158 3.2 54.2 1.0
CD2 B:HIS107 3.2 50.6 1.0
ND1 B:HIS158 4.1 53.1 1.0
ND1 B:HIS107 4.2 49.6 1.0
CG B:HIS158 4.3 51.1 1.0
CG B:HIS107 4.3 48.0 1.0
CB B:ASP109 4.4 65.0 1.0
N B:ASP109 4.9 58.8 1.0

Reference:

I.J.Clifton, L.C.Hsueh, J.E.Baldwin, K.Harlos, C.J.Schofield. Structure of Proline 3-Hydroxylase. Evolution of the Family of 2-Oxoglutarate Dependent Oxygenases. Eur.J.Biochem. V. 268 6625 2001.
ISSN: ISSN 0014-2956
PubMed: 11737217
DOI: 10.1046/J.0014-2956.2001.02617.X
Page generated: Sat Aug 3 04:15:07 2024

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