Iron in PDB 4f0l: Crystal Structure of Amidohydrolase From Brucella Melitensis

The structure of Crystal Structure of Amidohydrolase From Brucella Melitensis, PDB code: 4f0l was solved by Seattle Structural Genomics Center For Infectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.05
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	53.592, 62.192, 68.926, 92.75, 95.49, 112.32
R / Rfree (%)	14.8 / 18.4

The binding sites of Iron atom in the Crystal Structure of Amidohydrolase From Brucella Melitensis (pdb code 4f0l). 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 Amidohydrolase From Brucella Melitensis, PDB code: 4f0l:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Amidohydrolase From Brucella Melitensis


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 Amidohydrolase From Brucella Melitensis within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:25.1 occ:1.00 O A:HOH937 1.9 27.7 1.0 NE2 A:HIS63 2.2 18.6 1.0 NE2 A:HIS61 2.2 13.3 1.0 NE2 A:HIS237 2.3 17.9 1.0 OD1 A:ASP325 2.4 13.4 1.0 O A:HOH777 2.5 27.7 1.0 CE1 A:HIS63 3.1 19.0 1.0 CD2 A:HIS61 3.1 12.7 1.0 CG A:ASP325 3.2 12.6 1.0 CD2 A:HIS63 3.2 17.6 1.0 CE1 A:HIS237 3.3 18.2 1.0 CE1 A:HIS61 3.3 13.5 1.0 CD2 A:HIS237 3.3 17.8 1.0 OD2 A:ASP325 3.5 13.6 1.0 O A:HOH957 3.7 37.8 1.0 O A:HOH839 4.0 24.3 1.0 O A:HOH942 4.0 34.3 1.0 NE2 A:HIS274 4.0 14.7 1.0 ND1 A:HIS63 4.3 19.1 1.0 CG A:HIS61 4.3 12.5 1.0 CG A:HIS63 4.3 17.0 1.0 ND1 A:HIS61 4.4 13.0 1.0 ND1 A:HIS237 4.4 18.1 1.0 CG A:HIS237 4.5 17.1 1.0 CB A:ASP325 4.5 11.6 1.0 O A:HOH849 4.6 30.2 1.0 CE1 A:HIS274 4.8 14.1 1.0 CG2 A:ILE273 4.8 12.1 1.0 CA A:ASP325 4.9 11.2 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Amidohydrolase From Brucella Melitensis


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 Amidohydrolase From Brucella Melitensis within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:32.8 occ:1.00 NE2 B:HIS61 2.2 13.7 1.0 O B:HOH769 2.2 26.0 1.0 NE2 B:HIS63 2.2 21.6 1.0 O B:HOH687 2.3 32.7 1.0 NE2 B:HIS237 2.4 25.4 1.0 OD1 B:ASP325 2.4 18.2 1.0 CD2 B:HIS61 3.0 13.5 1.0 CE1 B:HIS63 3.0 23.0 1.0 CD2 B:HIS63 3.2 21.1 1.0 CG B:ASP325 3.2 16.6 1.0 CE1 B:HIS61 3.2 14.2 1.0 CE1 B:HIS237 3.3 25.9 1.0 CD2 B:HIS237 3.3 25.3 1.0 OD2 B:ASP325 3.5 17.8 1.0 O B:HOH861 3.8 35.0 1.0 O B:HOH854 3.9 30.4 1.0 NE2 B:HIS274 4.1 18.4 1.0 ND1 B:HIS63 4.2 23.2 1.0 CG B:HIS61 4.3 13.4 1.0 ND1 B:HIS61 4.3 13.9 1.0 CG B:HIS63 4.3 20.3 1.0 ND1 B:HIS237 4.4 26.2 1.0 CG B:HIS237 4.5 24.0 1.0 CB B:ASP325 4.5 14.9 1.0 O B:HOH770 4.5 37.6 1.0 CG2 B:ILE273 4.8 15.6 1.0 CE1 B:HIS274 4.8 17.4 1.0 CA B:ASP325 4.9 14.5 1.0

A.S.Gardberg, J.Abendroth, B.Staker, L.Stewart, Seattle Structural Genomics Center For Infectious Disease(Ssgcid). Crystal Structure of Amidohydrolase From Brucella Melitensis To Be Published.