Atomistry » Magnesium » PDB 1pi3-1q24 » 1q0b
Atomistry »
  Magnesium »
    PDB 1pi3-1q24 »
      1q0b »

Magnesium in PDB 1q0b: Crystal Structure of the Motor Protein Ksp in Complex with Adp and Monastrol

Protein crystallography data

The structure of Crystal Structure of the Motor Protein Ksp in Complex with Adp and Monastrol, PDB code: 1q0b was solved by Y.Yan, V.Sardana, B.Xu, W.Halczenko, C.Homnick, C.A.Buser, G.D.Hartman, H.E.Huber, L.C.Kuo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 69.300, 79.500, 159.200, 90.00, 90.00, 90.00
R / Rfree (%) 21.9 / 24.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Motor Protein Ksp in Complex with Adp and Monastrol (pdb code 1q0b). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the Motor Protein Ksp in Complex with Adp and Monastrol, PDB code: 1q0b:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1q0b

Go back to Magnesium Binding Sites List in 1q0b
Magnesium binding site 1 out of 2 in the Crystal Structure of the Motor Protein Ksp in Complex with Adp and Monastrol


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the Motor Protein Ksp in Complex with Adp and Monastrol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg603

b:15.6
occ:1.00
O3B A:ADP601 2.2 10.3 1.0
O A:HOH606 2.2 10.9 1.0
OG1 A:THR112 2.2 9.5 1.0
O A:HOH610 2.3 9.5 1.0
O A:HOH789 2.3 9.5 1.0
O A:HOH702 2.3 11.0 1.0
CB A:THR112 3.2 10.5 1.0
PB A:ADP601 3.3 10.0 1.0
O1B A:ADP601 3.5 9.9 1.0
N A:THR112 3.9 8.9 1.0
O2A A:ADP601 3.9 16.4 1.0
CA A:THR112 4.1 8.8 1.0
O A:SER232 4.2 14.9 1.0
OD2 A:ASP265 4.2 19.5 1.0
CG2 A:THR112 4.3 15.6 1.0
O A:HOH705 4.3 11.7 1.0
O A:HOH760 4.3 24.9 1.0
O3A A:ADP601 4.3 11.9 1.0
O A:HOH666 4.3 15.8 1.0
O A:HOH713 4.4 22.4 1.0
O A:HOH618 4.4 13.3 1.0
O2B A:ADP601 4.4 11.4 1.0
OD1 A:ASP265 4.5 17.8 1.0
PA A:ADP601 4.6 15.6 1.0
CG A:ASP265 4.8 18.1 1.0
O1A A:ADP601 4.8 17.0 1.0
CB A:LYS111 4.9 9.5 1.0
NZ A:LYS111 5.0 9.3 1.0
CE A:LYS111 5.0 11.1 1.0

Magnesium binding site 2 out of 2 in 1q0b

Go back to Magnesium Binding Sites List in 1q0b
Magnesium binding site 2 out of 2 in the Crystal Structure of the Motor Protein Ksp in Complex with Adp and Monastrol


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the Motor Protein Ksp in Complex with Adp and Monastrol within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg602

b:18.9
occ:1.00
OG1 B:THR112 2.2 12.2 1.0
O3B B:ADP600 2.2 10.9 1.0
O B:HOH795 2.2 9.6 1.0
O B:HOH615 2.3 11.1 1.0
O B:HOH609 2.3 12.5 1.0
O B:HOH628 2.3 9.9 1.0
CB B:THR112 3.2 11.7 1.0
PB B:ADP600 3.3 11.6 1.0
O1B B:ADP600 3.4 12.1 1.0
O2A B:ADP600 3.9 18.4 1.0
N B:THR112 3.9 10.2 1.0
O B:HOH724 4.1 28.4 1.0
CA B:THR112 4.1 10.7 1.0
O B:SER232 4.2 15.8 1.0
O B:HOH716 4.2 13.3 1.0
CG2 B:THR112 4.2 14.6 1.0
OD2 B:ASP265 4.3 18.0 1.0
O3A B:ADP600 4.3 14.9 1.0
O B:HOH674 4.3 28.6 1.0
O B:HOH685 4.4 20.8 1.0
O B:HOH627 4.4 10.9 1.0
O2B B:ADP600 4.5 13.1 1.0
OD1 B:ASP265 4.5 19.2 1.0
PA B:ADP600 4.6 16.6 1.0
O1A B:ADP600 4.8 15.8 1.0
CG B:ASP265 4.8 18.2 1.0
CB B:LYS111 4.9 9.5 1.0
CE B:LYS111 5.0 12.8 1.0

Reference:

Y.Yan, V.Sardana, B.Xu, C.Homnick, W.Halczenko, C.A.Buser, M.Schaber, G.D.Hartman, H.E.Huber, L.C.Kuo. Inhibition of A Mitotic Motor Protein: Where, How, and Conformational Consequences J.Mol.Biol. V. 335 547 2004.
ISSN: ISSN 0022-2836
PubMed: 14672662
DOI: 10.1016/J.JMB.2003.10.074
Page generated: Tue Aug 13 10:59:08 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy