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Magnesium in PDB 7lc1: Crystal Structure of KRAS4B (Gmppnp-Bound) in Complex with the Rbd-pH Domains of SIN1

Enzymatic activity of Crystal Structure of KRAS4B (Gmppnp-Bound) in Complex with the Rbd-pH Domains of SIN1

All present enzymatic activity of Crystal Structure of KRAS4B (Gmppnp-Bound) in Complex with the Rbd-pH Domains of SIN1:
3.6.5.2;

Protein crystallography data

The structure of Crystal Structure of KRAS4B (Gmppnp-Bound) in Complex with the Rbd-pH Domains of SIN1, PDB code: 7lc1 was solved by S.Dharmaiah, D.K.Simanshu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.54 / 2.35
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.76, 97.07, 96.62, 90, 92.32, 90
R / Rfree (%) 23.1 / 27.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of KRAS4B (Gmppnp-Bound) in Complex with the Rbd-pH Domains of SIN1 (pdb code 7lc1). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of KRAS4B (Gmppnp-Bound) in Complex with the Rbd-pH Domains of SIN1, PDB code: 7lc1:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 7lc1

Go back to Magnesium Binding Sites List in 7lc1
Magnesium binding site 1 out of 2 in the Crystal Structure of KRAS4B (Gmppnp-Bound) in Complex with the Rbd-pH Domains of SIN1


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 KRAS4B (Gmppnp-Bound) in Complex with the Rbd-pH Domains of SIN1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg201

b:40.6
occ:1.00
OG A:SER17 1.7 45.7 1.0
OG1 A:THR35 1.8 43.7 1.0
O3G A:GNP202 2.0 43.6 1.0
O A:HOH307 2.0 39.8 1.0
O1B A:GNP202 2.0 41.4 1.0
O A:HOH304 2.1 35.1 1.0
CB A:SER17 3.0 41.4 1.0
CB A:THR35 3.0 41.1 1.0
PG A:GNP202 3.1 30.8 1.0
PB A:GNP202 3.2 35.2 1.0
N3B A:GNP202 3.3 47.8 1.0
N A:THR35 3.7 36.8 1.0
N A:SER17 3.7 32.3 1.0
OD2 A:ASP57 3.9 46.3 1.0
CA A:THR35 3.9 37.5 1.0
O1G A:GNP202 3.9 28.8 1.0
CA A:SER17 3.9 40.1 1.0
CG2 A:THR35 4.0 42.9 1.0
O1A A:GNP202 4.1 37.5 1.0
O3A A:GNP202 4.1 46.5 1.0
O2G A:GNP202 4.2 31.1 1.0
O A:ASP33 4.3 42.3 1.0
O2B A:GNP202 4.3 34.0 1.0
OD1 A:ASP57 4.3 41.2 1.0
PA A:GNP202 4.4 34.9 1.0
O A:HOH313 4.4 45.3 1.0
O2A A:GNP202 4.5 36.1 1.0
CG A:ASP57 4.5 43.2 1.0
O A:THR58 4.6 38.8 1.0
C A:PRO34 4.6 43.9 1.0
CB A:LYS16 4.8 34.4 1.0
C A:LYS16 4.8 35.6 1.0
CA A:PRO34 4.9 50.1 1.0
CE A:LYS16 4.9 35.7 1.0

Magnesium binding site 2 out of 2 in 7lc1

Go back to Magnesium Binding Sites List in 7lc1
Magnesium binding site 2 out of 2 in the Crystal Structure of KRAS4B (Gmppnp-Bound) in Complex with the Rbd-pH Domains of SIN1


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of KRAS4B (Gmppnp-Bound) in Complex with the Rbd-pH Domains of SIN1 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg201

b:54.5
occ:1.00
OG C:SER17 1.8 48.1 1.0
OG1 C:THR35 1.8 52.5 1.0
O C:HOH302 2.0 46.9 1.0
O C:HOH301 2.0 49.5 1.0
O1B C:GNP202 2.0 48.7 1.0
O1G C:GNP202 2.2 53.2 1.0
CB C:THR35 2.9 54.8 1.0
CB C:SER17 3.1 47.9 1.0
PB C:GNP202 3.2 43.5 1.0
PG C:GNP202 3.3 44.2 1.0
N3B C:GNP202 3.4 50.2 1.0
N C:SER17 3.7 47.2 1.0
N C:THR35 3.7 54.5 1.0
CA C:THR35 3.9 55.7 1.0
CA C:SER17 3.9 47.9 1.0
CG2 C:THR35 4.0 54.8 1.0
OD1 C:ASP57 4.0 50.3 1.0
O2G C:GNP202 4.0 48.4 1.0
O3A C:GNP202 4.2 57.6 1.0
O C:HOH303 4.2 56.9 1.0
O1A C:GNP202 4.3 49.1 1.0
O2B C:GNP202 4.3 51.4 1.0
O C:THR58 4.3 51.1 1.0
O3G C:GNP202 4.4 47.5 1.0
CG C:ASP57 4.5 51.9 1.0
OD2 C:ASP57 4.5 46.9 1.0
O C:ASP33 4.5 55.0 1.0
PA C:GNP202 4.5 44.1 1.0
O2A C:GNP202 4.6 39.0 1.0
C C:PRO34 4.7 61.6 1.0
CB C:LYS16 4.7 47.6 1.0
C C:LYS16 4.8 49.5 1.0
CE C:LYS16 4.9 51.6 1.0
CA C:PRO34 5.0 57.9 1.0

Reference:

P.Castel, S.Dharmaiah, M.J.Sale, S.Messing, G.Rizzuto, A.Cuevas-Navarro, A.Cheng, M.J.Trnka, A.Urisman, D.Esposito, D.K.Simanshu, F.Mccormick. Ras Interaction to SIN1 Is Dispensable For MTORC2 Assembly and Activity Proc.Natl.Acad.Sci.Usa 2021.
ISSN: ESSN 1091-6490
Page generated: Wed Oct 2 23:20:13 2024

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