Atomistry » Magnesium » PDB 4r0d-4rcr » 4r3a
Atomistry »
  Magnesium »
    PDB 4r0d-4rcr »
      4r3a »

Magnesium in PDB 4r3a: Erythrobacter Litoralis EL346 Blue-Light Activated Histidine Kinase

Enzymatic activity of Erythrobacter Litoralis EL346 Blue-Light Activated Histidine Kinase

All present enzymatic activity of Erythrobacter Litoralis EL346 Blue-Light Activated Histidine Kinase:
2.7.13.3;

Protein crystallography data

The structure of Erythrobacter Litoralis EL346 Blue-Light Activated Histidine Kinase, PDB code: 4r3a was solved by D.R.Tomchick, G.Rivera-Cancel, K.H.Gardner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.60 / 2.92
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 98.882, 98.882, 422.255, 90.00, 90.00, 120.00
R / Rfree (%) 29 / 33

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Erythrobacter Litoralis EL346 Blue-Light Activated Histidine Kinase (pdb code 4r3a). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Erythrobacter Litoralis EL346 Blue-Light Activated Histidine Kinase, PDB code: 4r3a:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 4r3a

Go back to Magnesium Binding Sites List in 4r3a
Magnesium binding site 1 out of 2 in the Erythrobacter Litoralis EL346 Blue-Light Activated Histidine Kinase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Erythrobacter Litoralis EL346 Blue-Light Activated Histidine Kinase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg400

b:24.8
occ:1.00
O2G A:ANP401 1.9 0.1 1.0
O1A A:ANP401 2.0 0.6 1.0
O2B A:ANP401 2.1 0.3 1.0
OD1 A:ASN250 2.1 73.6 1.0
HD21 A:ASN250 2.9 80.2 1.0
PB A:ANP401 2.9 39.0 1.0
CG A:ASN250 3.0 63.1 1.0
PA A:ANP401 3.0 0.7 1.0
O3A A:ANP401 3.0 89.7 1.0
PG A:ANP401 3.1 52.9 1.0
ND2 A:ASN250 3.2 66.8 1.0
N3B A:ANP401 3.4 0.8 1.0
HA3 A:GLY300 3.4 36.6 1.0
HNB1 A:ANP401 3.5 0.6 1.0
O3G A:ANP401 3.7 0.6 1.0
O5' A:ANP401 3.8 59.2 1.0
HE2 A:HIS254 3.8 67.5 1.0
HA A:ASN250 4.0 71.3 1.0
HD22 A:ASN250 4.1 80.2 1.0
O2A A:ANP401 4.3 0.4 1.0
O1G A:ANP401 4.3 34.8 1.0
CB A:ASN250 4.3 64.0 1.0
OE1 A:GLU246 4.3 58.7 1.0
O1B A:ANP401 4.3 25.6 1.0
CA A:GLY300 4.4 30.5 1.0
HG22 A:THR249 4.4 57.0 1.0
O A:GLU246 4.5 48.7 1.0
NE2 A:HIS254 4.5 56.3 1.0
HD2 A:HIS254 4.5 63.9 1.0
OE1 A:GLN253 4.5 55.7 1.0
CA A:ASN250 4.6 59.4 1.0
H A:GLY300 4.6 36.1 1.0
HA2 A:GLY300 4.8 36.6 1.0
HE1 A:TRP293 4.8 42.9 1.0
HB3 A:ASN250 4.8 76.8 1.0
HB2 A:ASN250 4.8 76.8 1.0
CD2 A:HIS254 4.8 53.2 1.0
H A:ASN250 4.8 60.2 1.0
N A:ASN250 4.9 50.1 1.0

Magnesium binding site 2 out of 2 in 4r3a

Go back to Magnesium Binding Sites List in 4r3a
Magnesium binding site 2 out of 2 in the Erythrobacter Litoralis EL346 Blue-Light Activated Histidine Kinase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Erythrobacter Litoralis EL346 Blue-Light Activated Histidine Kinase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg400

b:79.0
occ:1.00
O2G B:ANP401 2.0 42.4 1.0
O1A B:ANP401 2.0 0.8 1.0
OD1 B:ASN250 2.1 95.9 1.0
O2B B:ANP401 2.2 96.5 1.0
HD21 B:ASN250 2.8 0.9 1.0
CG B:ASN250 2.8 95.1 1.0
ND2 B:ASN250 3.1 94.1 1.0
PG B:ANP401 3.2 0.9 1.0
PA B:ANP401 3.3 0.5 1.0
PB B:ANP401 3.4 82.2 1.0
HE2 B:HIS254 3.5 0.3 1.0
O3G B:ANP401 3.5 45.8 1.0
HA3 B:GLY300 3.7 0.1 1.0
O3A B:ANP401 3.7 91.4 1.0
HA B:ASN250 3.7 0.8 1.0
HD22 B:ASN250 3.9 0.9 1.0
N3B B:ANP401 4.0 77.0 1.0
O5' B:ANP401 4.0 0.9 1.0
CB B:ASN250 4.1 95.5 1.0
HD2 B:HIS254 4.2 0.5 1.0
NE2 B:HIS254 4.2 0.3 1.0
CA B:ASN250 4.3 96.5 1.0
O B:GLU246 4.4 93.5 1.0
O1G B:ANP401 4.4 0.5 1.0
OE1 B:GLU246 4.4 94.3 1.0
O2A B:ANP401 4.5 0.5 1.0
CD2 B:HIS254 4.5 0.2 1.0
OE1 B:GLN253 4.5 0.1 1.0
HNB1 B:ANP401 4.6 92.4 1.0
HB2 B:ASN250 4.6 0.7 1.0
O1B B:ANP401 4.6 82.4 1.0
H3' B:ANP401 4.7 0.9 1.0
CA B:GLY300 4.7 0.3 1.0
H B:ASN250 4.7 0.9 1.0
HB3 B:ASN250 4.7 0.7 1.0
N B:ASN250 4.7 95.8 1.0
HE1 B:TRP293 4.8 0.7 1.0
H B:GLY300 4.9 0.5 1.0
H8 B:ANP401 4.9 0.7 1.0
HB B:THR249 4.9 0.6 1.0
HA2 B:GLY300 5.0 0.1 1.0

Reference:

G.Rivera-Cancel, W.-H.Ko, D.R.Tomchick, F.Correa, K.H.Gardner. Full-Length Structure of A Monomeric Histidine Kinase Reveals Basis For Sensory Regulation Proc.Natl.Acad.Sci.Usa 2014.
ISSN: ESSN 1091-6490
Page generated: Mon Dec 14 19:29:35 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy