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Magnesium in PDB 2p9s: Structure of Bovine ARP2/3 Complex Co-Crystallized with Atp/MG2+

Protein crystallography data

The structure of Structure of Bovine ARP2/3 Complex Co-Crystallized with Atp/MG2+, PDB code: 2p9s was solved by B.J.Nolen, T.D.Pollard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.68
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 111.020, 128.694, 201.402, 90.00, 90.00, 90.00
R / Rfree (%) 22.2 / 26.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Bovine ARP2/3 Complex Co-Crystallized with Atp/MG2+ (pdb code 2p9s). 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 Structure of Bovine ARP2/3 Complex Co-Crystallized with Atp/MG2+, PDB code: 2p9s:

Magnesium binding site 1 out of 1 in 2p9s

Go back to Magnesium Binding Sites List in 2p9s
Magnesium binding site 1 out of 1 in the Structure of Bovine ARP2/3 Complex Co-Crystallized with Atp/MG2+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Bovine ARP2/3 Complex Co-Crystallized with Atp/MG2+ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg500

b:43.4
occ:1.00
O1B A:ATP501 2.5 45.8 1.0
O A:HOH509 2.7 41.2 1.0
O2G A:ATP501 2.8 48.5 1.0
OE1 A:GLN144 3.5 51.8 1.0
O3G A:ATP501 3.8 49.4 1.0
PG A:ATP501 3.8 46.2 1.0
OD1 A:ASP11 3.8 41.0 1.0
PB A:ATP501 3.9 44.2 1.0
OD2 A:ASP11 3.9 40.9 1.0
NZ A:LYS18 4.2 31.0 1.0
CD A:GLN144 4.2 47.2 1.0
CG A:ASP11 4.3 40.5 1.0
O3B A:ATP501 4.3 46.0 1.0
CA A:GLY13 4.5 41.8 1.0
OD1 A:ASP169 4.5 55.3 1.0
OD2 A:ASP169 4.5 56.2 1.0
O1A A:ATP501 4.7 42.5 1.0
NE2 A:GLN144 4.7 46.3 1.0
O3A A:ATP501 4.8 43.4 1.0
O2B A:ATP501 4.9 44.3 1.0
CG A:ASP169 5.0 54.4 1.0

Reference:

B.J.Nolen, T.D.Pollard. Insights Into the Influence of Nucleotides on Actin Family Proteins From Seven Structures of ARP2/3 Complex. Mol.Cell V. 26 449 2007.
ISSN: ISSN 1097-2765
PubMed: 17499050
DOI: 10.1016/J.MOLCEL.2007.04.017
Page generated: Sun Aug 10 12:53:20 2025

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