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Magnesium in PDB 3hkc: Tubulin-ABT751: RB3 Stathmin-Like Domain Complex

Protein crystallography data

The structure of Tubulin-ABT751: RB3 Stathmin-Like Domain Complex, PDB code: 3hkc was solved by A.Dorleans, B.Gigant, R.B.G.Ravelli, P.Mailliet, V.Mikol, M.Knossow, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 3.80
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 329.240, 329.240, 53.870, 90.00, 90.00, 120.00
R / Rfree (%) 20.3 / 25.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Tubulin-ABT751: RB3 Stathmin-Like Domain Complex (pdb code 3hkc). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Tubulin-ABT751: RB3 Stathmin-Like Domain Complex, PDB code: 3hkc:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 3hkc

Go back to Magnesium Binding Sites List in 3hkc
Magnesium binding site 1 out of 3 in the Tubulin-ABT751: RB3 Stathmin-Like Domain Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Tubulin-ABT751: RB3 Stathmin-Like Domain Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg601

b:40.7
occ:1.00
O2B A:GTP600 1.6 47.8 1.0
O3G A:GTP600 2.2 51.2 1.0
CA A:GLY144 2.9 51.5 1.0
PB A:GTP600 2.9 49.8 1.0
N A:GLY144 3.1 51.3 1.0
CB A:ALA99 3.3 50.1 1.0
PG A:GTP600 3.3 50.6 1.0
N A:THR145 3.3 51.3 1.0
O3A A:GTP600 3.5 50.1 1.0
O3B A:GTP600 3.6 50.1 1.0
N A:ASN101 3.6 49.7 1.0
C A:GLY144 3.6 51.5 1.0
O2G A:GTP600 3.8 49.6 1.0
OD1 A:ASP98 3.8 52.8 1.0
N A:ALA100 3.9 50.4 1.0
CG2 A:THR145 3.9 51.6 1.0
O1B A:GTP600 4.1 50.3 1.0
CA A:ALA99 4.1 50.1 1.0
C A:ALA99 4.2 50.2 1.0
CA A:ASN101 4.2 49.4 1.0
N A:ALA99 4.3 50.2 1.0
C A:GLY143 4.3 51.2 1.0
OD1 A:ASN101 4.4 50.5 1.0
C A:ALA100 4.6 49.9 1.0
NZ B:LYS254 4.6 51.0 1.0
O1G A:GTP600 4.6 49.2 1.0
CA A:ALA100 4.6 50.2 1.0
CA A:THR145 4.6 51.3 1.0
O A:GLY144 4.8 51.6 1.0
CB A:THR145 4.8 51.5 1.0
O A:ALA99 4.8 50.0 1.0
CG A:ASP98 5.0 52.5 1.0

Magnesium binding site 2 out of 3 in 3hkc

Go back to Magnesium Binding Sites List in 3hkc
Magnesium binding site 2 out of 3 in the Tubulin-ABT751: RB3 Stathmin-Like Domain Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Tubulin-ABT751: RB3 Stathmin-Like Domain Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg601

b:48.0
occ:1.00
O2A B:GDP600 3.1 50.6 1.0
ND2 B:ASN101 3.2 52.8 1.0
OE1 C:GLU254 3.7 55.4 1.0
OE1 B:GLN11 4.3 52.5 1.0
O2B B:GDP600 4.4 52.1 1.0
CG B:ASN101 4.4 52.0 1.0
CD C:GLU254 4.5 54.7 1.0
PA B:GDP600 4.5 50.5 1.0
OE2 C:GLU254 4.7 55.0 1.0
OD1 B:ASN101 4.9 52.0 1.0
O3B B:GDP600 5.0 51.7 1.0

Magnesium binding site 3 out of 3 in 3hkc

Go back to Magnesium Binding Sites List in 3hkc
Magnesium binding site 3 out of 3 in the Tubulin-ABT751: RB3 Stathmin-Like Domain Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Tubulin-ABT751: RB3 Stathmin-Like Domain Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg601

b:41.7
occ:1.00
O2B C:GTP600 1.6 48.0 1.0
O3G C:GTP600 2.1 51.2 1.0
PB C:GTP600 2.9 49.2 1.0
CA C:GLY144 3.0 51.5 1.0
PG C:GTP600 3.1 50.5 1.0
CB C:ALA99 3.1 50.1 1.0
N C:GLY144 3.2 51.5 1.0
N C:THR145 3.4 51.3 1.0
O2G C:GTP600 3.4 49.8 1.0
O3B C:GTP600 3.5 49.8 1.0
O3A C:GTP600 3.5 50.0 1.0
N C:ASN101 3.7 49.6 1.0
C C:GLY144 3.7 51.5 1.0
OD1 C:ASP98 3.7 52.6 1.0
N C:ALA100 3.9 50.3 1.0
CG2 C:THR145 3.9 51.6 1.0
O1B C:GTP600 4.0 49.9 1.0
CA C:ALA99 4.1 50.1 1.0
NZ D:LYS254 4.1 50.9 1.0
C C:ALA99 4.2 50.1 1.0
N C:ALA99 4.3 50.2 1.0
CA C:ASN101 4.3 49.5 1.0
OD1 C:ASN101 4.4 50.5 1.0
O1G C:GTP600 4.4 49.5 1.0
C C:GLY143 4.5 51.3 1.0
CA C:THR145 4.7 51.1 1.0
CA C:ALA100 4.7 50.1 1.0
C C:ALA100 4.7 49.7 1.0
CB C:THR145 4.8 51.2 1.0
CG C:ASP98 4.9 52.4 1.0
O C:GLY144 4.9 51.7 1.0

Reference:

A.Dorleans, B.Gigant, R.B.G.Ravelli, P.Mailliet, V.Mikol, M.Knossow. Variations in the Colchicine-Binding Domain Provide Insight Into the Structural Switch of Tubulin Proc.Natl.Acad.Sci.Usa V. 106 13775 2009.
ISSN: ISSN 0027-8424
PubMed: 19666559
DOI: 10.1073/PNAS.0904223106
Page generated: Sun Aug 10 21:57:34 2025

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