Cobalt in PDB 4ero: Study on Structure and Function Relationships in Human Pirin with Cobalt Ion

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

The structure of Study on Structure and Function Relationships in Human Pirin with Cobalt Ion, PDB code: 4ero 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)	25.08 / 2.65
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	42.127, 66.254, 106.127, 90.00, 90.00, 90.00
R / Rfree (%)	19.2 / 23.5

The binding sites of Cobalt atom in the Study on Structure and Function Relationships in Human Pirin with Cobalt Ion (pdb code 4ero). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the Study on Structure and Function Relationships in Human Pirin with Cobalt Ion, PDB code: 4ero:

Cobalt binding site 1 out of 1 in the Study on Structure and Function Relationships in Human Pirin with Cobalt Ion


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Study on Structure and Function Relationships in Human Pirin with Cobalt Ion within 5.0Å range: probe atom residue distance (Å) B Occ A:Co1001 b:10.7 occ:1.00 NE2 A:HIS58 2.1 6.2 1.0 NE2 A:HIS101 2.3 8.9 1.0 NE2 A:HIS56 2.3 8.1 1.0 OE2 A:GLU103 2.9 9.8 1.0 CD2 A:HIS56 3.1 8.0 1.0 CE1 A:HIS58 3.1 6.4 1.0 CE1 A:HIS101 3.1 8.8 1.0 CD2 A:HIS58 3.1 6.3 1.0 CD2 A:HIS101 3.4 8.8 1.0 CE1 A:HIS56 3.4 8.0 1.0 CD A:GLU103 3.8 10.0 1.0 OE1 A:GLN115 4.1 2.0 0.9 ND1 A:HIS58 4.2 6.2 1.0 CG A:HIS58 4.3 6.1 1.0 ND1 A:HIS101 4.3 8.8 1.0 CG A:HIS56 4.3 8.0 1.0 OE1 A:GLU103 4.3 9.8 1.0 ND1 A:HIS56 4.4 8.0 1.0 CG A:HIS101 4.4 8.8 1.0 CG A:GLU103 4.8 9.9 1.0 OG1 A:THR63 4.9 2.0 1.0 CE A:MET93 5.0 2.0 0.9

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