Magnesium in PDB 6bbq: Model For Extended Volume of Truncated Monomeric Cytohesin-3 (GRP1; Amino Acids 63-399) E161A ARF6 Q67L Fusion Protein

The binding sites of Magnesium atom in the Model For Extended Volume of Truncated Monomeric Cytohesin-3 (GRP1; Amino Acids 63-399) E161A ARF6 Q67L Fusion Protein (pdb code 6bbq). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Model For Extended Volume of Truncated Monomeric Cytohesin-3 (GRP1; Amino Acids 63-399) E161A ARF6 Q67L Fusion Protein, PDB code: 6bbq:

Magnesium binding site 1 out of 1 in the Model For Extended Volume of Truncated Monomeric Cytohesin-3 (GRP1; Amino Acids 63-399) E161A ARF6 Q67L Fusion Protein


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Model For Extended Volume of Truncated Monomeric Cytohesin-3 (GRP1; Amino Acids 63-399) E161A ARF6 Q67L Fusion Protein within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg602 b:20.0 occ:1.00 O3G A:GTP601 2.0 20.0 1.0 OG1 A:THR425 2.0 20.0 1.0 O2B A:GTP601 2.1 20.0 1.0 OG1 A:THR442 2.2 20.0 1.0 PG A:GTP601 3.1 20.0 1.0 CB A:THR425 3.2 20.0 1.0 CB A:THR442 3.2 20.0 1.0 PB A:GTP601 3.3 20.0 1.0 O3B A:GTP601 3.5 20.0 1.0 O1G A:GTP601 3.6 20.0 1.0 N A:THR442 3.9 20.0 1.0 N A:THR425 3.9 20.0 1.0 OD2 A:ASP461 4.0 20.0 1.0 O2A A:GTP601 4.1 20.0 1.0 CA A:THR425 4.1 20.0 1.0 CA A:THR442 4.2 20.0 1.0 CG2 A:THR425 4.2 20.0 1.0 OD1 A:ASP461 4.3 20.0 1.0 CG2 A:THR442 4.3 20.0 1.0 O3A A:GTP601 4.3 20.0 1.0 O1B A:GTP601 4.3 20.0 1.0 O2G A:GTP601 4.4 20.0 1.0 ND2 A:ASN446 4.5 20.0 1.0 O A:ILE440 4.5 20.0 1.0 PA A:GTP601 4.5 20.0 1.0 CG A:ASP461 4.6 20.0 1.0 O1A A:GTP601 4.7 20.0 1.0 C A:PRO441 4.8 20.0 1.0 CB A:LYS424 4.9 20.0 1.0

A.W.Malaby, S.Das, S.Chakravarthy, T.C.Irving, O.Bilsel, D.G.Lambright. Structural Dynamics Control Allosteric Activation of Cytohesin Family Arf Gtpase Exchange Factors. Structure V. 26 106 2018.
ISSN: ISSN 1878-4186
PubMed: 29276036
DOI: 10.1016/J.STR.2017.11.019