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Magnesium in PDB 7p52: GLNK1 From Methanocaldococcus Jannaschii with Mg-Atp and 2- Oxoglutarate at A Resolution of 1.2 A

Protein crystallography data

The structure of GLNK1 From Methanocaldococcus Jannaschii with Mg-Atp and 2- Oxoglutarate at A Resolution of 1.2 A, PDB code: 7p52 was solved by M.-C.Mueller, T.Wagner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.53 / 1.20
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 89.053, 89.053, 98.059, 90, 90, 120
R / Rfree (%) 13.1 / 15.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the GLNK1 From Methanocaldococcus Jannaschii with Mg-Atp and 2- Oxoglutarate at A Resolution of 1.2 A (pdb code 7p52). 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 GLNK1 From Methanocaldococcus Jannaschii with Mg-Atp and 2- Oxoglutarate at A Resolution of 1.2 A, PDB code: 7p52:

Magnesium binding site 1 out of 1 in 7p52

Go back to Magnesium Binding Sites List in 7p52
Magnesium binding site 1 out of 1 in the GLNK1 From Methanocaldococcus Jannaschii with Mg-Atp and 2- Oxoglutarate at A Resolution of 1.2 A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of GLNK1 From Methanocaldococcus Jannaschii with Mg-Atp and 2- Oxoglutarate at A Resolution of 1.2 A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg305

b:12.9
occ:1.00
O1G A:ATP301 2.0 13.3 1.0
O1B A:ATP301 2.0 13.2 1.0
OE1 A:GLN39 2.0 15.8 1.0
O2 A:AKG302 2.1 13.0 1.0
O5 A:AKG302 2.1 16.1 1.0
O1A A:ATP301 2.1 14.2 1.0
C1 A:AKG302 2.9 13.0 1.0
C2 A:AKG302 3.0 13.6 1.0
PB A:ATP301 3.1 13.0 1.0
PG A:ATP301 3.2 14.0 1.0
CD A:GLN39 3.2 16.1 1.0
PA A:ATP301 3.3 12.6 1.0
O3A A:ATP301 3.5 11.0 1.0
O3B A:ATP301 3.5 13.5 1.0
N A:GLY87 3.7 13.9 1.0
O3G A:ATP301 3.8 13.8 1.0
NE2 A:GLN39 3.9 17.5 1.0
N A:VAL38 4.0 14.5 1.0
O2A A:ATP301 4.0 13.2 1.0
O1 A:AKG302 4.1 16.0 1.0
O A:HOH451 4.1 14.9 1.0
CA A:GLY37 4.1 12.1 1.0
CA A:GLY87 4.2 13.4 1.0
N A:GLN39 4.2 16.7 1.0
CB A:PRO86 4.2 17.7 1.0
C A:GLY37 4.3 14.1 1.0
C A:PRO86 4.3 15.3 1.0
CG A:GLN39 4.4 17.7 1.0
N A:GLY37 4.4 13.2 1.0
CB A:GLN39 4.4 16.7 1.0
C3 A:AKG302 4.4 15.0 1.0
O5' A:ATP301 4.4 12.0 1.0
O2G A:ATP301 4.5 14.2 1.0
O2B A:ATP301 4.5 12.2 1.0
CA A:PRO86 4.6 15.8 1.0
CG2 A:VAL38 4.7 17.0 0.5
CA A:VAL38 4.9 15.3 0.5
CB A:VAL38 4.9 16.1 0.5
C4 A:AKG302 4.9 16.2 1.0
CA A:GLN39 5.0 16.9 1.0
CA A:VAL38 5.0 15.3 0.5

Reference:

M.C.Muller, T.Wagner. The Oxoglutarate Binding Site and Regulatory Mechanism Are Conserved in Ammonium Transporter Inhibitors Glnks From Methanococcales . Int J Mol Sci V. 22 2021.
ISSN: ESSN 1422-0067
PubMed: 34445335
DOI: 10.3390/IJMS22168631
Page generated: Thu Oct 3 04:01:23 2024

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