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Magnesium in PDB 1mkj: Human Kinesin Motor Domain with Docked Neck Linker

Protein crystallography data

The structure of Human Kinesin Motor Domain with Docked Neck Linker, PDB code: 1mkj was solved by C.V.Sindelar, M.J.Budny, S.Rice, N.Naber, R.Fletterick, R.Cooke, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.03 / 2.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 73.796, 74.086, 91.543, 90.00, 90.00, 90.00
R / Rfree (%) 20.9 / 25.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Human Kinesin Motor Domain with Docked Neck Linker (pdb code 1mkj). 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 Human Kinesin Motor Domain with Docked Neck Linker, PDB code: 1mkj:

Magnesium binding site 1 out of 1 in 1mkj

Go back to Magnesium Binding Sites List in 1mkj
Magnesium binding site 1 out of 1 in the Human Kinesin Motor Domain with Docked Neck Linker


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human Kinesin Motor Domain with Docked Neck Linker within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg400

b:30.4
occ:1.00
O2B A:ADP600 2.5 29.1 1.0
OG1 A:THR92 2.6 14.9 1.0
O3B A:ADP600 3.3 27.0 1.0
PB A:ADP600 3.5 21.1 1.0
CB A:THR92 3.8 13.6 1.0
O2A A:ADP600 4.1 33.8 1.0
OD1 A:ASP231 4.4 37.2 1.0
N A:THR92 4.5 13.2 1.0
O3A A:ADP600 4.5 30.0 1.0
O1B A:ADP600 4.5 25.1 1.0
O A:SER201 4.7 16.6 1.0
CA A:THR92 4.7 14.1 1.0
CG2 A:THR92 4.8 12.4 1.0
OD2 A:ASP231 4.8 35.0 1.0
CE A:LYS91 4.8 7.3 1.0
NZ A:LYS91 4.9 7.0 1.0
PA A:ADP600 4.9 31.1 1.0
CB A:SER201 4.9 15.5 1.0
OG A:SER201 4.9 15.4 1.0
CG A:ASP231 5.0 32.4 1.0
C A:SER201 5.0 16.3 1.0

Reference:

C.V.Sindelar, M.J.Budny, S.Rice, N.Naber, R.Fletterick, R.Cooke. Two Conformations in the Human Kinesin Power Stroke Defined By X-Ray Crystallography and Epr Spectroscopy. Nat.Struct.Biol. V. 9 844 2002.
ISSN: ISSN 1072-8368
PubMed: 12368902
Page generated: Sun Aug 10 01:06:08 2025

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