Iron in PDB 2ivp: Structure of UP1 Protein

All present enzymatic activity of Structure of UP1 Protein:
3.4.24.57;

The structure of Structure of UP1 Protein, PDB code: 2ivp was solved by A.Hecker, N.Leulliot, M.Graille, P.Dorlet, S.Quevillon-Cheruel, N.Ulryck, H.Van Tilbeurgh, P.Forterre, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.5
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	61.688, 69.914, 74.306, 90.00, 90.00, 90.00
R / Rfree (%)	21.8 / 27.7

The binding sites of Iron atom in the Structure of UP1 Protein (pdb code 2ivp). 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 Structure of UP1 Protein, PDB code: 2ivp:

Iron binding site 1 out of 1 in the Structure of UP1 Protein


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of UP1 Protein within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1326 b:74.7 occ:1.00 NE2 A:HIS107 2.2 28.9 1.0 OD1 A:ASP285 2.3 30.2 1.0 OH A:TYR127 2.4 27.4 1.0 O1G A:ATP1327 2.5 40.0 1.0 NE2 A:HIS111 2.6 23.0 1.0 O2G A:ATP1327 3.0 40.5 1.0 PG A:ATP1327 3.1 40.3 1.0 CE1 A:HIS107 3.2 27.8 1.0 CD2 A:HIS107 3.2 27.1 1.0 CZ A:TYR127 3.3 26.5 1.0 CG A:ASP285 3.4 28.5 1.0 CD2 A:HIS111 3.4 23.5 1.0 O3B A:ATP1327 3.4 37.8 1.0 CE1 A:HIS111 3.4 22.4 1.0 CE1 A:TYR127 3.5 26.1 1.0 OD2 A:ASP285 3.8 31.3 1.0 OG A:SER129 4.1 29.8 1.0 O2A A:ATP1327 4.3 32.5 1.0 ND1 A:HIS107 4.3 27.1 1.0 CB A:SER129 4.4 27.7 1.0 CG A:HIS107 4.4 25.9 1.0 ND1 A:HIS111 4.4 23.0 1.0 CG A:HIS111 4.5 22.8 1.0 OD1 A:ASN132 4.5 29.7 1.0 CE2 A:TYR127 4.5 26.5 1.0 O3G A:ATP1327 4.6 40.3 1.0 CB A:ASP285 4.7 27.2 1.0 CA A:ASP285 4.8 27.0 1.0 CD1 A:TYR127 4.8 26.4 1.0 N A:ASP285 4.8 26.9 1.0 PB A:ATP1327 5.0 35.0 1.0

A.Hecker, N.Leulliot, D.Gadelle, M.Graille, A.Justome, P.Dorlet, C.Brochier, S.Quevillon-Cheruel, E.Le Cam, H.Van Tilbeurgh, P.Forterre. An Archaeal Orthologue of the Universal Protein KAE1 Is An Iron Metalloprotein Which Exhibits Atypical Dna-Binding Properties and Apurinic- Endonuclease Activity in Vitro. Nucleic Acids Res. V. 35 6042 2007.
ISSN: ISSN 0305-1048
PubMed: 17766251
DOI: 10.1093/NAR/GKM554