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Sodium in PDB 4mao: RSK2 T493M C-Terminal Kinase Domain in Complex with RMM58

Enzymatic activity of RSK2 T493M C-Terminal Kinase Domain in Complex with RMM58

All present enzymatic activity of RSK2 T493M C-Terminal Kinase Domain in Complex with RMM58:
2.7.11.1;

Protein crystallography data

The structure of RSK2 T493M C-Terminal Kinase Domain in Complex with RMM58, PDB code: 4mao was solved by R.M.Miller, J.Taunton, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.12 / 2.60
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 47.500, 47.500, 288.500, 90.00, 90.00, 90.00
R / Rfree (%) 23.5 / 29.2

Sodium Binding Sites:

The binding sites of Sodium atom in the RSK2 T493M C-Terminal Kinase Domain in Complex with RMM58 (pdb code 4mao). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the RSK2 T493M C-Terminal Kinase Domain in Complex with RMM58, PDB code: 4mao:

Sodium binding site 1 out of 1 in 4mao

Go back to Sodium Binding Sites List in 4mao
Sodium binding site 1 out of 1 in the RSK2 T493M C-Terminal Kinase Domain in Complex with RMM58


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of RSK2 T493M C-Terminal Kinase Domain in Complex with RMM58 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na802

b:39.9
occ:1.00
O A:ILE476 2.3 40.5 1.0
O A:GLY471 2.3 41.2 1.0
O A:HIS473 2.3 41.6 1.0
OG1 A:THR478 2.5 44.3 1.0
C A:HIS473 3.3 41.1 1.0
C A:GLY471 3.5 37.4 1.0
C A:ILE476 3.5 39.8 1.0
HA A:THR478 3.6 51.4 1.0
HA A:PRO474 3.7 47.2 1.0
H A:ILE476 3.7 46.8 1.0
CB A:THR478 3.8 44.3 1.0
C A:GLN472 3.8 44.9 1.0
O A:GLN472 3.8 44.3 1.0
HB A:ILE476 3.9 45.6 1.0
CA A:THR478 4.0 42.9 1.0
N A:HIS473 4.0 43.5 1.0
N A:THR478 4.0 44.6 1.0
HA A:GLN472 4.1 58.8 1.0
C A:ILE477 4.1 40.3 1.0
N A:PRO474 4.1 41.1 1.0
CA A:PRO474 4.1 39.4 1.0
C A:PRO474 4.2 38.9 1.0
O A:ILE477 4.2 37.3 1.0
O A:PRO474 4.2 39.8 1.0
N A:ILE476 4.2 39.0 1.0
HA2 A:GLY471 4.3 45.6 1.0
CA A:GLN472 4.3 49.0 1.0
CA A:HIS473 4.3 44.6 1.0
CA A:ILE476 4.3 36.4 1.0
HG23 A:THR478 4.3 55.3 1.0
N A:GLN472 4.3 41.4 1.0
H A:HIS473 4.4 52.2 1.0
H A:THR478 4.4 53.5 1.0
HB A:THR478 4.4 53.1 1.0
N A:ILE477 4.5 37.6 1.0
CA A:GLY471 4.5 38.0 1.0
HA A:ILE477 4.5 43.3 1.0
CB A:ILE476 4.5 38.0 1.0
CG2 A:THR478 4.6 46.1 1.0
HG22 A:ILE476 4.6 41.1 1.0
CA A:ILE477 4.6 36.1 1.0
HB3 A:HIS473 4.7 49.7 1.0
OE1 A:GLU494 4.7 45.1 1.0
HG21 A:THR478 4.8 55.3 1.0
N A:ASN475 4.8 40.2 1.0
HA3 A:GLY471 4.8 45.6 1.0
HD2 A:ARG558 4.8 49.5 1.0
HE A:ARG558 4.9 48.9 1.0
HD3 A:ARG558 5.0 49.5 1.0

Reference:

S.Krishnan, R.M.Miller, B.Tian, R.D.Mullins, M.P.Jacobson, J.Taunton. Design of Reversible, Cysteine-Targeted Michael Acceptors Guided By Kinetic and Computational Analysis. J.Am.Chem.Soc. V. 136 12624 2014.
ISSN: ISSN 0002-7863
PubMed: 25153195
DOI: 10.1021/JA505194W
Page generated: Tue Dec 15 06:54:00 2020

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