Iron in PDB 2o6a: Crystal Structure of the Haemophilus Influenzae E57A Mutant Fbpa

The structure of Crystal Structure of the Haemophilus Influenzae E57A Mutant Fbpa, PDB code: 2o6a was solved by S.R.Shouldice, L.W.Tari, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.80
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	106.065, 75.230, 33.369, 90.00, 90.00, 90.00
R / Rfree (%)	20.2 / 25

The binding sites of Iron atom in the Crystal Structure of the Haemophilus Influenzae E57A Mutant Fbpa (pdb code 2o6a). 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 Crystal Structure of the Haemophilus Influenzae E57A Mutant Fbpa, PDB code: 2o6a:

Iron binding site 1 out of 1 in the Crystal Structure of the Haemophilus Influenzae E57A Mutant Fbpa


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 the Haemophilus Influenzae E57A Mutant Fbpa within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:42.9 occ:1.00 OH A:TYR196 1.5 31.6 1.0 O A:HOH582 2.1 31.3 1.0 O2 A:PO4402 2.1 48.2 1.0 O A:HOH492 2.3 56.3 1.0 CZ A:TYR196 2.8 27.4 1.0 O A:HOH504 3.0 50.8 1.0 P A:PO4402 3.3 48.5 1.0 CE1 A:TYR196 3.6 26.9 1.0 O3 A:PO4402 3.6 50.7 1.0 O A:HOH455 3.6 52.1 1.0 OH A:TYR195 3.7 24.8 1.0 ND2 A:ASN175 3.8 23.3 1.0 CE2 A:TYR196 3.8 26.2 1.0 O A:HOH554 3.8 69.5 1.0 O A:HOH624 3.9 52.4 1.0 O4 A:PO4402 4.0 50.2 1.0 O A:HOH439 4.1 20.6 1.0 O A:HOH622 4.3 48.2 1.0 O1 A:PO4402 4.4 48.0 1.0 CE2 A:TYR195 4.4 23.1 1.0 CZ A:TYR195 4.5 23.1 1.0 ND2 A:ASN193 4.6 19.5 1.0 O A:HOH545 4.8 42.3 1.0 CG A:ASN175 4.8 21.1 1.0 CB A:ASN175 4.9 20.4 1.0 CD1 A:TYR196 4.9 25.8 1.0

A.G.Khan, S.R.Shouldice, S.D.Kirby, R.H.Yu, L.W.Tari, A.B.Schryvers. High-Affinity Binding By the Periplasmic Iron-Binding Protein From Haemophilus Influenzae Is Required For Acquiring Iron From Transferrin Biochem.J. V. 404 217 2007.
ISSN: ISSN 0264-6021
PubMed: 17313366
DOI: 10.1042/BJ20070110