Iron in PDB 4gul: Study on Structure and Function Relationships in Human Ferric Pirin

All present enzymatic activity of Study on Structure and Function Relationships in Human Ferric Pirin:
1.13.11.24;

The structure of Study on Structure and Function Relationships in Human Ferric Pirin, PDB code: 4gul was solved by F.Liu, I.Rehmani, R.Fu, S.Esaka, L.Chen, V.Serrano, A.Liu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	21.87 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	42.305, 67.031, 107.058, 90.00, 90.00, 90.00
R / Rfree (%)	18.7 / 23.4

The binding sites of Iron atom in the Study on Structure and Function Relationships in Human Ferric Pirin (pdb code 4gul). 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 Study on Structure and Function Relationships in Human Ferric Pirin, PDB code: 4gul:

Iron binding site 1 out of 1 in the Study on Structure and Function Relationships in Human Ferric Pirin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Study on Structure and Function Relationships in Human Ferric Pirin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1001 b:13.4 occ:1.00 NE2 A:HIS101 2.1 15.6 1.0 NE2 A:HIS56 2.2 12.0 1.0 NE2 A:HIS58 2.2 14.5 1.0 O A:HOH1261 2.2 22.7 1.0 O A:HOH1262 2.3 21.2 1.0 OE2 A:GLU103 2.4 19.8 1.0 CE1 A:HIS101 3.1 14.1 1.0 CE1 A:HIS56 3.1 12.9 1.0 CE1 A:HIS58 3.2 15.2 1.0 CD2 A:HIS101 3.2 13.8 1.0 CD2 A:HIS58 3.2 14.7 1.0 CD2 A:HIS56 3.2 13.0 1.0 CD A:GLU103 3.4 22.7 1.0 OE1 A:GLU103 3.8 25.0 1.0 ND1 A:HIS101 4.2 16.1 1.0 ND1 A:HIS56 4.3 12.6 1.0 CG A:HIS101 4.3 13.1 1.0 ND1 A:HIS58 4.3 16.9 1.0 NE2 A:GLN115 4.3 15.6 1.0 CG A:HIS56 4.3 12.7 1.0 CG A:HIS58 4.3 15.2 1.0 CG A:GLU103 4.6 17.8 1.0 OG1 A:THR63 4.9 18.0 1.0

F.Liu, I.Rehmani, S.Esaki, R.Fu, L.Chen, V.De Serrano, A.Liu. Pirin Is An Iron-Dependent Redox Regulator of Nf-Kappa B. Proc.Natl.Acad.Sci.Usa V. 110 9722 2013.
ISSN: ISSN 0027-8424
PubMed: 23716661
DOI: 10.1073/PNAS.1221743110