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Magnesium in PDB 1rfq: Actin Crystal Dynamics: Structural Implications For F-Actin Nucleation, Polymerization and Branching Mediated By the Anti-Parallel Dimer

Protein crystallography data

The structure of Actin Crystal Dynamics: Structural Implications For F-Actin Nucleation, Polymerization and Branching Mediated By the Anti-Parallel Dimer, PDB code: 1rfq was solved by R.Reutzel, C.Yoshioka, L.Govindasamy, E.G.Yarmola, M.Agbandje-Mckenna, M.R.Bubb, R.Mckenna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 3.00
Space group P 43
Cell size a, b, c (Å), α, β, γ (°) 101.500, 101.500, 104.200, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / 26.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Actin Crystal Dynamics: Structural Implications For F-Actin Nucleation, Polymerization and Branching Mediated By the Anti-Parallel Dimer (pdb code 1rfq). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Actin Crystal Dynamics: Structural Implications For F-Actin Nucleation, Polymerization and Branching Mediated By the Anti-Parallel Dimer, PDB code: 1rfq:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1rfq

Go back to Magnesium Binding Sites List in 1rfq
Magnesium binding site 1 out of 2 in the Actin Crystal Dynamics: Structural Implications For F-Actin Nucleation, Polymerization and Branching Mediated By the Anti-Parallel Dimer


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Actin Crystal Dynamics: Structural Implications For F-Actin Nucleation, Polymerization and Branching Mediated By the Anti-Parallel Dimer within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg378

b:36.2
occ:1.00
O3G A:ATP376 2.2 41.9 1.0
NE2 A:GLN137 2.6 53.8 1.0
O2B A:ATP376 2.7 42.2 1.0
OD2 A:ASP154 3.2 56.2 1.0
PG A:ATP376 3.4 42.5 1.0
CD A:GLN137 3.7 53.5 1.0
PB A:ATP376 3.8 41.6 1.0
O1G A:ATP376 3.8 37.7 1.0
O3B A:ATP376 3.9 40.2 1.0
O1A A:ATP376 4.1 47.1 1.0
CA A:GLY156 4.2 48.1 1.0
OD1 A:ASP11 4.2 51.9 1.0
OE1 A:GLN137 4.2 54.1 1.0
O3A A:ATP376 4.3 43.6 1.0
CG A:ASP154 4.3 55.3 1.0
OD2 A:ASP11 4.4 50.1 1.0
PA A:ATP376 4.4 47.2 1.0
N A:GLY156 4.5 50.9 1.0
CG A:GLN137 4.6 49.0 1.0
O2G A:ATP376 4.7 41.0 1.0
CA A:GLY13 4.7 45.0 1.0
CG2 A:VAL339 4.8 37.8 1.0
CG A:ASP11 4.8 50.8 1.0
CA A:GLY301 4.9 49.4 1.0
CB A:GLN137 4.9 44.6 1.0
CB A:ASP154 4.9 53.7 1.0

Magnesium binding site 2 out of 2 in 1rfq

Go back to Magnesium Binding Sites List in 1rfq
Magnesium binding site 2 out of 2 in the Actin Crystal Dynamics: Structural Implications For F-Actin Nucleation, Polymerization and Branching Mediated By the Anti-Parallel Dimer


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Actin Crystal Dynamics: Structural Implications For F-Actin Nucleation, Polymerization and Branching Mediated By the Anti-Parallel Dimer within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg388

b:42.2
occ:1.00
O2B B:ATP386 2.2 56.4 1.0
CA B:GLY13 2.6 63.5 1.0
O1G B:ATP386 2.9 61.3 1.0
O3G B:ATP386 3.0 59.1 1.0
OE1 B:GLN137 3.0 59.3 1.0
PB B:ATP386 3.2 55.7 1.0
PG B:ATP386 3.3 62.2 1.0
N B:GLY13 3.4 63.7 1.0
O3B B:ATP386 3.4 57.7 1.0
OD2 B:ASP11 3.5 65.6 1.0
C B:GLY13 3.7 64.0 1.0
N B:SER14 3.7 64.0 1.0
NZ B:LYS18 3.7 60.3 1.0
CD B:GLN137 3.9 58.6 1.0
CG B:ASP11 4.0 65.3 1.0
OD1 B:ASP11 4.0 65.7 1.0
OD2 B:ASP154 4.1 63.6 1.0
O3A B:ATP386 4.3 54.6 1.0
O1B B:ATP386 4.4 53.5 1.0
C B:ASN12 4.5 63.9 1.0
NE2 B:GLN137 4.6 57.4 1.0
PA B:ATP386 4.7 55.1 1.0
CG B:GLN137 4.7 56.4 1.0
CE B:LYS18 4.7 59.3 1.0
O2G B:ATP386 4.7 59.9 1.0
O B:GLY13 4.9 62.5 1.0
OG B:SER14 4.9 58.5 1.0
O B:ASN12 5.0 64.2 1.0

Reference:

R.Reutzel, C.Yoshioka, L.Govindasamy, E.G.Yarmola, M.Agbandje-Mckenna, M.R.Bubb, R.Mckenna. Actin Crystal Dynamics: Structural Implications For F-Actin Nucleation, Polymerization, and Branching Mediated By the Anti-Parallel Dimer. J.Struct.Biol. V. 146 291 2004.
ISSN: ISSN 1047-8477
PubMed: 15099571
DOI: 10.1016/J.JSB.2003.12.006
Page generated: Tue Aug 13 12:59:29 2024

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