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Magnesium in PDB 5idj: Bifunctional Histidine Kinase Ccka (Domains Dhp-Ca) in Complex with Adp/MG2+

Protein crystallography data

The structure of Bifunctional Histidine Kinase Ccka (Domains Dhp-Ca) in Complex with Adp/MG2+, PDB code: 5idj was solved by B.N.Dubey, T.Schirmer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 3.01
Space group P 63 2 2
Cell size a, b, c (Å), α, β, γ (°) 164.856, 164.856, 48.001, 90.00, 90.00, 120.00
R / Rfree (%) 21.2 / 27.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Bifunctional Histidine Kinase Ccka (Domains Dhp-Ca) in Complex with Adp/MG2+ (pdb code 5idj). 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 Bifunctional Histidine Kinase Ccka (Domains Dhp-Ca) in Complex with Adp/MG2+, PDB code: 5idj:

Magnesium binding site 1 out of 1 in 5idj

Go back to Magnesium Binding Sites List in 5idj
Magnesium binding site 1 out of 1 in the Bifunctional Histidine Kinase Ccka (Domains Dhp-Ca) in Complex with Adp/MG2+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Bifunctional Histidine Kinase Ccka (Domains Dhp-Ca) in Complex with Adp/MG2+ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg601

b:61.4
occ:1.00
O1A A:ADP600 2.3 67.8 1.0
OD1 A:ASN434 2.3 67.2 1.0
O3B A:ADP600 3.0 59.2 1.0
O2B A:ADP600 3.2 68.4 1.0
CG A:ASN434 3.5 69.7 1.0
PB A:ADP600 3.6 62.8 1.0
PA A:ADP600 3.7 61.2 1.0
ND2 A:ASN434 4.0 68.3 1.0
O3A A:ADP600 4.2 44.1 1.0
CA A:GLY509 4.3 58.3 1.0
O A:ASN430 4.5 68.6 1.0
N A:GLY509 4.6 59.5 1.0
O5' A:ADP600 4.7 59.8 1.0
CB A:ASN434 4.7 72.9 1.0
O2A A:ADP600 4.7 60.9 1.0
N A:ASN434 4.8 71.5 1.0
CA A:ASN434 4.8 74.4 1.0
CG1 A:VAL433 4.8 71.6 1.0
O1B A:ADP600 5.0 67.7 1.0

Reference:

B.N.Dubey, C.Lori, S.Ozaki, G.Fucile, I.Plaza-Menacho, U.Jenal, T.Schirmer. Cyclic Di-Gmp Mediates A Histidine Kinase/Phosphatase Switch By Noncovalent Domain Cross-Linking. Sci Adv V. 2 00823 2016.
ISSN: ESSN 2375-2548
PubMed: 27652341
DOI: 10.1126/SCIADV.1600823
Page generated: Sun Sep 29 16:40:31 2024

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