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Magnesium in PDB 5l3q: Structure of the Gtpase Heterodimer of Human SRP54 and Sralpha

Protein crystallography data

The structure of Structure of the Gtpase Heterodimer of Human SRP54 and Sralpha, PDB code: 5l3q was solved by K.Wild, B.Segnitz, I.Sinning, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 76.34 / 3.20
Space group I 2 3
Cell size a, b, c (Å), α, β, γ (°) 241.394, 241.394, 241.394, 90.00, 90.00, 90.00
R / Rfree (%) 14.5 / 19.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of the Gtpase Heterodimer of Human SRP54 and Sralpha (pdb code 5l3q). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Structure of the Gtpase Heterodimer of Human SRP54 and Sralpha, PDB code: 5l3q:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 5l3q

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Magnesium binding site 1 out of 4 in the Structure of the Gtpase Heterodimer of Human SRP54 and Sralpha


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the Gtpase Heterodimer of Human SRP54 and Sralpha within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg503

b:30.9
occ:1.00
N3B A:GNP502 2.0 47.7 1.0
O A:HOH609 2.1 34.2 1.0
O A:HOH610 2.1 19.9 1.0
O A:HOH601 2.1 11.6 1.0
OG1 A:THR115 2.2 38.7 1.0
O1B A:GNP502 2.5 43.6 1.0
O2G A:GNP502 2.7 38.5 1.0
PG A:GNP502 2.9 39.9 1.0
PB A:GNP502 2.9 39.2 1.0
CB A:THR115 3.3 39.5 1.0
O3G A:GNP502 3.9 40.6 1.0
O1G A:GNP502 3.9 39.2 1.0
O3A A:GNP502 4.0 36.8 1.0
N A:THR115 4.0 41.1 1.0
O2B A:GNP502 4.0 38.7 1.0
CD A:ARG141 4.1 40.1 1.0
O2A A:GNP502 4.2 39.5 1.0
CA A:THR115 4.2 40.1 1.0
CG2 A:THR115 4.3 41.6 1.0
PA A:GNP502 4.3 37.3 1.0
OD2 A:ASP190 4.4 39.6 1.0
O1A A:GNP502 4.4 37.5 1.0
O A:HOH616 4.4 37.2 1.0
OD2 A:ASP138 4.4 49.3 1.0
CE A:LYS114 4.5 39.4 1.0
OE1 A:GLN147 4.6 40.1 1.0
NZ A:LYS114 4.6 35.8 1.0
NE A:ARG141 4.7 45.9 1.0
OD1 A:ASP190 4.7 43.4 1.0
NH1 A:ARG141 4.8 44.9 1.0
O A:THR191 4.8 46.1 1.0
CB A:LYS114 4.9 38.8 1.0
CZ A:ARG141 5.0 45.6 1.0

Magnesium binding site 2 out of 4 in 5l3q

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Magnesium binding site 2 out of 4 in the Structure of the Gtpase Heterodimer of Human SRP54 and Sralpha


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of the Gtpase Heterodimer of Human SRP54 and Sralpha within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg706

b:28.8
occ:1.00
O B:HOH805 2.0 94.3 1.0
O B:HOH819 2.1 27.1 1.0
O B:HOH804 2.1 15.6 1.0
OG B:SER432 2.1 28.3 1.0
O2G B:GNP705 2.2 36.3 1.0
O2B B:GNP705 2.4 35.5 1.0
CB B:SER432 3.2 28.2 1.0
PG B:GNP705 3.5 34.9 1.0
PB B:GNP705 3.6 34.6 1.0
O B:HOH830 3.6 25.9 1.0
OD1 B:ASP520 3.7 47.6 1.0
N B:SER432 3.7 30.9 1.0
N3B B:GNP705 3.8 55.7 1.0
OD2 B:ASP520 4.0 47.4 1.0
CA B:SER432 4.0 29.8 1.0
OD2 B:ASP455 4.2 44.7 1.0
NH1 B:ARG458 4.2 33.5 1.0
CG B:ASP520 4.2 46.6 1.0
O1G B:GNP705 4.2 33.7 1.0
O B:THR521 4.3 42.1 1.0
O1B B:GNP705 4.4 31.8 1.0
CE B:LYS431 4.4 33.5 1.0
CB B:LYS431 4.4 31.6 1.0
OE1 B:GLN464 4.5 37.8 1.0
O B:HOH816 4.5 34.0 1.0
O1A B:GNP705 4.6 35.2 1.0
O3G B:GNP705 4.7 35.3 1.0
NZ B:LYS431 4.7 33.4 1.0
O3A B:GNP705 4.8 36.9 1.0
C B:LYS431 4.8 32.9 1.0
CB B:ASP455 5.0 39.4 1.0

Magnesium binding site 3 out of 4 in 5l3q

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Magnesium binding site 3 out of 4 in the Structure of the Gtpase Heterodimer of Human SRP54 and Sralpha


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Structure of the Gtpase Heterodimer of Human SRP54 and Sralpha within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg504

b:40.3
occ:1.00
O C:HOH602 2.1 65.8 1.0
OG1 C:THR115 2.1 55.0 1.0
O C:HOH601 2.1 50.5 1.0
O C:HOH603 2.1 36.9 1.0
O1B C:GNP503 2.3 49.5 1.0
O1G C:GNP503 2.4 39.5 1.0
CB C:THR115 3.0 48.0 1.0
PG C:GNP503 3.5 38.4 1.0
N3B C:GNP503 3.5 42.4 1.0
PB C:GNP503 3.5 45.9 1.0
O C:HOH608 3.8 74.2 1.0
OE1 C:GLN147 3.9 49.9 1.0
CG2 C:THR115 3.9 48.7 1.0
O2A C:GNP503 4.1 49.2 1.0
OD2 C:ASP138 4.1 63.6 1.0
CD C:ARG141 4.1 45.7 1.0
N C:THR115 4.1 53.4 1.0
CA C:THR115 4.1 53.5 1.0
OD2 C:ASP190 4.2 62.6 1.0
O2G C:GNP503 4.4 38.6 1.0
O1A C:GNP503 4.4 49.2 1.0
PA C:GNP503 4.5 48.1 1.0
O3A C:GNP503 4.5 45.8 1.0
O2B C:GNP503 4.5 44.0 1.0
NH1 C:ARG141 4.6 45.3 1.0
CD C:GLN147 4.6 50.0 1.0
OD1 C:ASP190 4.6 63.6 1.0
NE C:ARG141 4.6 49.3 1.0
O3G C:GNP503 4.7 35.4 1.0
NE2 C:GLN147 4.7 51.3 1.0
CZ C:ARG141 4.8 48.2 1.0
CG C:ASP190 4.9 61.9 1.0
O C:HOH611 5.0 36.9 1.0

Magnesium binding site 4 out of 4 in 5l3q

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Magnesium binding site 4 out of 4 in the Structure of the Gtpase Heterodimer of Human SRP54 and Sralpha


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Structure of the Gtpase Heterodimer of Human SRP54 and Sralpha within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg704

b:24.4
occ:1.00
O1G D:GNP703 2.0 35.9 1.0
O D:HOH808 2.1 34.7 1.0
O D:HOH812 2.1 21.9 1.0
O D:HOH804 2.1 16.0 1.0
OG D:SER432 2.2 30.5 1.0
O1B D:GNP703 2.3 33.5 1.0
CB D:SER432 3.2 39.4 1.0
PG D:GNP703 3.4 36.5 1.0
NH1 D:ARG458 3.5 46.3 1.0
PB D:GNP703 3.6 35.8 1.0
N3B D:GNP703 3.7 57.9 1.0
O D:HOH803 3.9 35.4 1.0
OD2 D:ASP455 3.9 52.3 1.0
N D:SER432 4.0 39.5 1.0
O D:HOH829 4.0 56.1 1.0
OE1 D:GLN464 4.1 38.6 1.0
OD2 D:ASP520 4.1 44.3 1.0
CA D:SER432 4.1 38.8 1.0
OD1 D:ASP520 4.1 44.8 1.0
O2G D:GNP703 4.2 35.9 1.0
O2B D:GNP703 4.4 36.7 1.0
O3G D:GNP703 4.5 38.4 1.0
CG D:ASP520 4.5 42.8 1.0
O1A D:GNP703 4.5 38.4 1.0
CZ D:ARG458 4.6 45.9 1.0
O3A D:GNP703 4.7 37.7 1.0
O2A D:GNP703 4.7 42.1 1.0
O D:THR521 4.8 37.4 1.0
PA D:GNP703 4.8 40.3 1.0
CB D:LYS431 4.9 36.5 1.0
CE D:LYS431 4.9 37.4 1.0
NH2 D:ARG458 4.9 48.9 1.0
CG D:ASP455 4.9 50.7 1.0
CD D:GLN464 4.9 39.0 1.0
CB D:ASP455 5.0 46.3 1.0

Reference:

K.Wild, G.Bange, D.Motiejunas, J.Kribelbauer, A.Hendricks, B.Segnitz, R.C.Wade, I.Sinning. Structural Basis For Conserved Regulation and Adaptation of the Signal Recognition Particle Targeting Complex. J.Mol.Biol. V. 428 2880 2016.
ISSN: ESSN 1089-8638
PubMed: 27241309
DOI: 10.1016/J.JMB.2016.05.015
Page generated: Mon Dec 14 20:38:43 2020

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