Manganese in PDB 1nr0: Two Seven-Bladed Beta-Propeller Domains Revealed By the Structure of A C. Elegans Homologue of Yeast Actin Interacting Protein 1 (AIP1).

The structure of Two Seven-Bladed Beta-Propeller Domains Revealed By the Structure of A C. Elegans Homologue of Yeast Actin Interacting Protein 1 (AIP1)., PDB code: 1nr0 was solved by S.M.Vorobiev, K.Mohri, S.Ono, S.C.Almo, S.K.Burley, New York Sgxresearch Center For Structural Genomics (Nysgxrc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	23.59 / 1.70
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	64.845, 65.174, 69.240, 90.00, 98.28, 90.00
R / Rfree (%)	19.9 / 23

The binding sites of Manganese atom in the Two Seven-Bladed Beta-Propeller Domains Revealed By the Structure of A C. Elegans Homologue of Yeast Actin Interacting Protein 1 (AIP1). (pdb code 1nr0). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Two Seven-Bladed Beta-Propeller Domains Revealed By the Structure of A C. Elegans Homologue of Yeast Actin Interacting Protein 1 (AIP1)., PDB code: 1nr0:

Manganese binding site 1 out of 1 in the Two Seven-Bladed Beta-Propeller Domains Revealed By the Structure of A C. Elegans Homologue of Yeast Actin Interacting Protein 1 (AIP1).


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Two Seven-Bladed Beta-Propeller Domains Revealed By the Structure of A C. Elegans Homologue of Yeast Actin Interacting Protein 1 (AIP1). within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn700 b:42.9 occ:1.00 O A:HOH1016 2.3 25.6 1.0 OD1 A:ASP154 2.3 14.9 1.0 O A:HOH839 2.3 17.5 1.0 O A:HOH1411 2.4 51.0 1.0 O A:HOH864 2.5 15.9 1.0 O A:HOH1159 2.6 37.1 1.0 CG A:ASP154 3.2 13.3 1.0 OD2 A:ASP154 3.4 15.3 1.0 O A:HOH1023 3.8 25.9 1.0 O A:HOH1361 3.9 40.6 1.0 O A:HOH831 4.1 13.7 1.0 OG A:SER110 4.2 11.8 1.0 O A:HOH933 4.3 18.9 1.0 O A:PHE155 4.3 14.9 1.0 O A:HOH1214 4.5 40.5 1.0 CB A:ASP154 4.5 11.8 1.0 O A:HOH1012 4.6 20.0 1.0 N A:PHE155 4.6 14.0 1.0 O A:HOH1316 4.7 25.4 1.0 O A:HOH806 4.7 12.6 1.0 O A:HOH1121 4.8 28.6 1.0 O A:HOH1378 4.8 40.3 1.0 O A:TRP111 4.8 12.6 1.0 CA A:ASP154 4.9 10.6 1.0

K.Mohri, S.M.Vorobiev, A.A.Fedorov, S.C.Almo, S.Ono. Identification of Functional Residues on Caenorhabditis Elegans Actin-Interacting Protein 1 (Unc-78) For Disassembly of Actin Depolymerizing Factor/Cofilin-Bound Actin Filaments J.Biol.Chem. V. 279 31697 2004.
ISSN: ISSN 0021-9258
PubMed: 15150269
DOI: 10.1074/JBC.M403351200