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Magnesium in PDB 5yee: Crystal Structure of LOKIPROFILIN1/Rabbit Actin Complex

Protein crystallography data

The structure of Crystal Structure of LOKIPROFILIN1/Rabbit Actin Complex, PDB code: 5yee was solved by R.C.Robinson, C.Akil, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 63.10 / 1.81
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 43.312, 126.209, 53.862, 90.00, 97.89, 90.00
R / Rfree (%) 19.1 / 24.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of LOKIPROFILIN1/Rabbit Actin Complex (pdb code 5yee). 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 LOKIPROFILIN1/Rabbit Actin Complex, PDB code: 5yee:

Magnesium binding site 1 out of 1 in 5yee

Go back to Magnesium Binding Sites List in 5yee
Magnesium binding site 1 out of 1 in the Crystal Structure of LOKIPROFILIN1/Rabbit Actin Complex


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 LOKIPROFILIN1/Rabbit Actin Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg403

b:10.4
occ:1.00
O B:HOH676 2.2 23.5 1.0
O3G B:ATP402 2.3 21.4 1.0
O2B B:ATP402 2.3 18.4 1.0
O B:HOH557 2.4 19.6 1.0
PG B:ATP402 3.5 21.0 1.0
PB B:ATP402 3.6 19.4 1.0
O3B B:ATP402 3.8 19.1 1.0
O1G B:ATP402 4.0 17.1 1.0
O B:HOH650 4.1 34.9 1.0
OE1 B:GLN137 4.1 18.9 1.0
O B:HOH547 4.1 23.6 1.0
O3A B:ATP402 4.2 19.7 1.0
CA B:GLY13 4.3 22.4 1.0
NZ B:LYS18 4.3 23.1 1.0
O B:HOH527 4.4 29.1 1.0
O2A B:ATP402 4.5 21.7 1.0
CD B:GLN137 4.5 18.8 1.0
OD2 B:ASP154 4.7 23.6 1.0
PA B:ATP402 4.8 22.0 1.0
OD2 B:ASP11 4.8 19.2 1.0
O2G B:ATP402 4.8 21.2 1.0
OD1 B:ASP11 4.8 18.9 1.0
O1B B:ATP402 4.9 20.4 1.0
NE2 B:GLN137 4.9 19.2 1.0

Reference:

C.Akil, R.C.Robinson. Genomes of Asgard Archaea Encode Profilins That Regulate Actin. Nature V. 562 439 2018.
ISSN: ESSN 1476-4687
PubMed: 30283132
DOI: 10.1038/S41586-018-0548-6
Page generated: Mon Sep 30 11:05:56 2024

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