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Magnesium in PDB 1nm1: Crystal Structure of D. Dicsoideum Actin Complexed with Gelsolin Segment 1 and Mg Atp at 1.8 A Resolution

Protein crystallography data

The structure of Crystal Structure of D. Dicsoideum Actin Complexed with Gelsolin Segment 1 and Mg Atp at 1.8 A Resolution, PDB code: 1nm1 was solved by S.M.Vorobiev, S.Welti, J.Condeelis, S.C.Almo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.80
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 178.539, 69.089, 56.552, 90.00, 104.34, 90.00
R / Rfree (%) 19.7 / 23.2

Other elements in 1nm1:

The structure of Crystal Structure of D. Dicsoideum Actin Complexed with Gelsolin Segment 1 and Mg Atp at 1.8 A Resolution also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of D. Dicsoideum Actin Complexed with Gelsolin Segment 1 and Mg Atp at 1.8 A Resolution (pdb code 1nm1). 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 Crystal Structure of D. Dicsoideum Actin Complexed with Gelsolin Segment 1 and Mg Atp at 1.8 A Resolution, PDB code: 1nm1:

Magnesium binding site 1 out of 1 in 1nm1

Go back to Magnesium Binding Sites List in 1nm1
Magnesium binding site 1 out of 1 in the Crystal Structure of D. Dicsoideum Actin Complexed with Gelsolin Segment 1 and Mg Atp at 1.8 A Resolution


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 D. Dicsoideum Actin Complexed with Gelsolin Segment 1 and Mg Atp at 1.8 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg403

b:35.9
occ:1.00
O A:HOH411 2.2 15.2 1.0
O2G A:ATP401 2.2 23.7 1.0
O A:HOH418 2.2 15.5 1.0
O A:HOH445 2.4 19.6 1.0
O A:HOH417 2.6 19.9 1.0
O1B A:ATP401 2.6 18.4 1.0
PG A:ATP401 3.3 20.9 1.0
PB A:ATP401 3.5 16.1 1.0
O3B A:ATP401 3.6 19.2 1.0
O A:HOH588 3.7 28.7 1.0
O3G A:ATP401 3.7 16.8 1.0
O A:HOH444 4.0 23.9 1.0
O3A A:ATP401 4.1 16.8 1.0
OE1 A:GLN137 4.2 14.6 1.0
O1A A:ATP401 4.2 16.3 1.0
OD1 A:ASP11 4.3 14.3 1.0
O A:HOH426 4.4 25.9 1.0
CA A:GLY13 4.4 14.9 1.0
OD2 A:ASP11 4.5 12.6 1.0
O A:HOH457 4.6 26.1 1.0
CD A:GLN137 4.6 17.2 1.0
NZ A:LYS18 4.6 14.7 1.0
O1G A:ATP401 4.6 18.9 1.0
PA A:ATP401 4.7 17.1 1.0
O2B A:ATP401 4.7 19.1 1.0
OD1 A:ASP154 4.8 27.7 1.0
CG A:ASP11 4.8 11.2 1.0
O A:HOH504 4.8 34.3 1.0
OD2 A:ASP154 4.9 30.4 1.0

Reference:

S.M.Vorobiev, B.Strokopytov, D.G.Drubin, C.Frieden, S.Ono, J.Condeelis, P.A.Rubenstein, S.C.Almo. The Structure of Non-Vertebrate Actin: Implications For the Atp Hydrolytic Mechanism Proc.Natl.Acad.Sci.Usa V. 100 5760 2003.
ISSN: ISSN 0027-8424
PubMed: 12732734
DOI: 10.1073/PNAS.0832273100
Page generated: Tue Aug 13 10:06:31 2024

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