Magnesium in PDB 5hnz: Structural Basis of Backwards Motion in Kinesin-14: Plus-End Directed NKN669 in the Nucleotide-Free State

The binding sites of Magnesium atom in the Structural Basis of Backwards Motion in Kinesin-14: Plus-End Directed NKN669 in the Nucleotide-Free State (pdb code 5hnz). 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 Structural Basis of Backwards Motion in Kinesin-14: Plus-End Directed NKN669 in the Nucleotide-Free State, PDB code: 5hnz:

Magnesium binding site 1 out of 1 in the Structural Basis of Backwards Motion in Kinesin-14: Plus-End Directed NKN669 in the Nucleotide-Free State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structural Basis of Backwards Motion in Kinesin-14: Plus-End Directed NKN669 in the Nucleotide-Free State within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:18.6 occ:1.00 CB A:GLN11 2.4 23.6 1.0 O1G A:GTP502 2.4 28.7 1.0 O1B A:GTP502 3.2 41.2 1.0 N A:GLN11 3.2 25.1 1.0 CA A:GLN11 3.2 23.8 1.0 OD2 A:ASP69 3.2 31.7 1.0 OE2 A:GLU71 3.4 47.9 1.0 OD1 A:ASP69 3.5 33.2 1.0 CG A:GLN11 3.6 24.7 1.0 CG2 A:VAL74 3.6 61.8 1.0 PG A:GTP502 3.7 30.0 1.0 O3B A:GTP502 3.7 35.2 1.0 CG A:ASP69 3.7 34.8 1.0 CD A:GLN11 3.8 29.2 1.0 PB A:GTP502 3.8 41.4 1.0 O3A A:GTP502 4.1 39.2 1.0 OE1 A:GLN11 4.2 33.8 1.0 NE2 A:GLN11 4.2 29.5 1.0 CB A:GLU71 4.3 46.4 1.0 CB A:VAL74 4.4 59.5 1.0 O2A A:GTP502 4.4 44.5 1.0 C A:GLY10 4.5 28.3 1.0 O2G A:GTP502 4.5 35.0 1.0 OD1 B:ASN249 4.5 37.8 1.0 C A:GLN11 4.5 23.9 1.0 CD A:GLU71 4.6 48.7 1.0 CG1 A:VAL74 4.7 60.8 1.0 PA A:GTP502 4.8 41.3 1.0 O3G A:GTP502 4.9 32.1 1.0 N A:ALA12 4.9 21.3 1.0 ND2 B:ASN249 5.0 36.7 1.0

M.Yamagishi, H.Shigematsu, T.Yokoyama, M.Kikkawa, M.Sugawa, M.Aoki, M.Shirouzu, J.Yajima, R.Nitta. Structural Basis of Backwards Motion in Kinesin-1-Kinesin-14 Chimera: Implication For Kinesin-14 Motility Structure V. 24 1322 2016.
ISSN: ISSN 0969-2126
PubMed: 27452403
DOI: 10.1016/J.STR.2016.05.021