Iron in PDB 4fil: Structure of FHUD2 From Staphylococcus Aureus with Bound Ferrioxamine B

The structure of Structure of FHUD2 From Staphylococcus Aureus with Bound Ferrioxamine B, PDB code: 4fil was solved by L.K.Briere, D.E.Heinrichs, B.H.Shilton, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.00 / 2.40
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	81.343, 78.996, 116.811, 90.00, 109.87, 90.00
R / Rfree (%)	19.8 / 22.9

The structure of Structure of FHUD2 From Staphylococcus Aureus with Bound Ferrioxamine B also contains other interesting chemical elements:

Zinc

(Zn)

56 atoms

The binding sites of Iron atom in the Structure of FHUD2 From Staphylococcus Aureus with Bound Ferrioxamine B (pdb code 4fil). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Structure of FHUD2 From Staphylococcus Aureus with Bound Ferrioxamine B, PDB code: 4fil:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Structure of FHUD2 From Staphylococcus Aureus with Bound Ferrioxamine B


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of FHUD2 From Staphylococcus Aureus with Bound Ferrioxamine B within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:32.9 occ:1.00 FE A:0UE401 0.0 32.9 1.0 O21 A:0UE401 2.0 40.6 1.0 O11 A:0UE401 2.0 38.9 1.0 O31 A:0UE401 2.0 35.6 1.0 O32 A:0UE401 2.0 19.9 1.0 O22 A:0UE401 2.0 45.7 1.0 O12 A:0UE401 2.0 36.7 1.0 C31 A:0UE401 2.8 39.8 1.0 C21 A:0UE401 2.8 52.8 1.0 N21 A:0UE401 2.8 36.8 1.0 N31 A:0UE401 2.8 43.5 1.0 N11 A:0UE401 2.8 28.6 1.0 C11 A:0UE401 2.8 38.9 1.0 C19 A:0UE401 4.2 24.9 1.0 C39 A:0UE401 4.2 26.8 1.0 C29 A:0UE401 4.2 34.5 1.0 NE1 A:TRP197 4.2 26.7 1.0 C22 A:0UE401 4.2 42.2 1.0 C32 A:0UE401 4.2 55.4 1.0 C12 A:0UE401 4.3 23.5 1.0 NH2 A:ARG199 4.3 24.2 1.0 NH1 A:ARG199 4.4 23.5 1.0 C40 A:0UE401 4.5 25.7 1.0 C28 A:0UE401 4.7 21.0 1.0 C18 A:0UE401 4.7 25.8 1.0 C27 A:0UE401 4.8 29.6 1.0 C23 A:0UE401 4.8 29.4 1.0 CZ A:ARG199 4.9 27.0 1.0 C17 A:0UE401 4.9 40.8 1.0 CD1 A:TRP197 4.9 22.6 1.0 C24 A:0UE401 5.0 40.2 1.0 N22 A:0UE401 5.0 36.9 1.0

Iron binding site 2 out of 4 in the Structure of FHUD2 From Staphylococcus Aureus with Bound Ferrioxamine B


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of FHUD2 From Staphylococcus Aureus with Bound Ferrioxamine B within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe401 b:30.5 occ:1.00 FE B:0UE401 0.0 30.5 1.0 O21 B:0UE401 2.0 38.7 1.0 O11 B:0UE401 2.0 25.9 1.0 O31 B:0UE401 2.0 29.6 1.0 O32 B:0UE401 2.0 67.3 1.0 O22 B:0UE401 2.0 41.8 1.0 O12 B:0UE401 2.0 45.6 1.0 C31 B:0UE401 2.8 49.1 1.0 C21 B:0UE401 2.8 53.2 1.0 N31 B:0UE401 2.8 38.7 1.0 N21 B:0UE401 2.8 51.0 1.0 N11 B:0UE401 2.8 19.8 1.0 C11 B:0UE401 2.8 30.7 1.0 NE1 B:TRP197 3.9 25.6 1.0 C19 B:0UE401 4.2 33.2 1.0 C39 B:0UE401 4.2 25.5 1.0 C29 B:0UE401 4.2 48.5 1.0 C22 B:0UE401 4.2 28.2 1.0 C32 B:0UE401 4.2 42.3 1.0 C12 B:0UE401 4.2 31.2 1.0 NH2 B:ARG199 4.3 28.1 1.0 NH1 B:ARG199 4.3 24.2 1.0 C40 B:0UE401 4.5 19.6 1.0 O A:HOH593 4.5 31.4 1.0 O B:HOH611 4.6 28.4 1.0 C27 B:0UE401 4.7 28.6 1.0 CD1 B:TRP197 4.7 19.5 1.0 CE2 B:TRP197 4.7 20.3 1.0 C28 B:0UE401 4.7 29.1 1.0 C17 B:0UE401 4.7 41.2 1.0 C18 B:0UE401 4.8 33.8 1.0 CZ B:ARG199 4.8 25.5 1.0 CZ2 B:TRP197 4.9 20.3 1.0 C23 B:0UE401 4.9 39.3 1.0 N22 B:0UE401 5.0 39.5 1.0

Iron binding site 3 out of 4 in the Structure of FHUD2 From Staphylococcus Aureus with Bound Ferrioxamine B


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Structure of FHUD2 From Staphylococcus Aureus with Bound Ferrioxamine B within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe401 b:34.7 occ:1.00 FE C:0UE401 0.0 34.7 1.0 O21 C:0UE401 2.0 70.2 1.0 O11 C:0UE401 2.0 50.0 1.0 O31 C:0UE401 2.0 34.8 1.0 O32 C:0UE401 2.0 49.9 1.0 O22 C:0UE401 2.0 45.9 1.0 O12 C:0UE401 2.0 31.0 1.0 C31 C:0UE401 2.8 48.2 1.0 C21 C:0UE401 2.8 40.3 1.0 N31 C:0UE401 2.8 31.9 1.0 N21 C:0UE401 2.8 40.5 1.0 N11 C:0UE401 2.8 37.8 1.0 C11 C:0UE401 2.8 32.9 1.0 NE1 C:TRP197 4.0 24.0 1.0 O C:HOH543 4.2 17.5 1.0 C39 C:0UE401 4.2 28.4 1.0 C19 C:0UE401 4.2 43.4 1.0 C29 C:0UE401 4.2 31.4 1.0 C22 C:0UE401 4.2 35.5 1.0 C32 C:0UE401 4.2 52.4 1.0 C12 C:0UE401 4.3 40.1 1.0 NH2 C:ARG199 4.3 26.5 1.0 NH1 C:ARG199 4.4 29.2 1.0 C40 C:0UE401 4.6 45.9 1.0 C17 C:0UE401 4.6 26.0 1.0 C27 C:0UE401 4.6 28.9 1.0 CD1 C:TRP197 4.6 20.1 1.0 C28 C:0UE401 4.7 42.8 1.0 CZ C:ARG199 4.9 25.1 1.0 C23 C:0UE401 4.9 38.5 1.0 C24 C:0UE401 5.0 55.2 1.0

Iron binding site 4 out of 4 in the Structure of FHUD2 From Staphylococcus Aureus with Bound Ferrioxamine B


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Structure of FHUD2 From Staphylococcus Aureus with Bound Ferrioxamine B within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe401 b:36.0 occ:1.00 FE D:0UE401 0.0 36.0 1.0 O21 D:0UE401 2.0 41.2 1.0 O11 D:0UE401 2.0 41.2 1.0 O31 D:0UE401 2.0 33.0 1.0 O32 D:0UE401 2.0 61.5 1.0 O22 D:0UE401 2.0 37.5 1.0 O12 D:0UE401 2.0 40.9 1.0 C31 D:0UE401 2.8 60.8 1.0 N11 D:0UE401 2.8 29.6 1.0 C21 D:0UE401 2.8 37.9 1.0 N31 D:0UE401 2.8 48.2 1.0 N21 D:0UE401 2.8 42.5 1.0 C11 D:0UE401 2.8 34.5 1.0 NE1 D:TRP197 4.0 25.7 1.0 C39 D:0UE401 4.1 24.9 1.0 C19 D:0UE401 4.2 39.1 1.0 C29 D:0UE401 4.2 23.1 1.0 C12 D:0UE401 4.2 30.1 1.0 C32 D:0UE401 4.2 45.9 1.0 C22 D:0UE401 4.2 30.8 1.0 NH2 D:ARG199 4.4 28.6 1.0 C40 D:0UE401 4.4 31.7 1.0 NH1 D:ARG199 4.4 26.2 1.0 O D:HOH551 4.5 38.7 1.0 C28 D:0UE401 4.7 29.2 1.0 C27 D:0UE401 4.7 41.7 1.0 CD1 D:TRP197 4.8 19.0 1.0 C18 D:0UE401 4.8 41.5 1.0 CE2 D:TRP197 4.8 23.1 1.0 C17 D:0UE401 4.9 53.4 1.0 CZ D:ARG199 4.9 23.1 1.0 C23 D:0UE401 4.9 38.9 1.0

K.J.Podkowa, L.A.Briere, D.E.Heinrichs, B.H.Shilton. Crystal and Solution Structure Analysis of FHUD2 From Staphylococcus Aureus in Multiple Unliganded Conformations and Bound to Ferrioxamine-B. Biochemistry V. 53 2017 2014.
ISSN: ISSN 0006-2960
PubMed: 24606332
DOI: 10.1021/BI401349D