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Magnesium in PDB 7mss: Human E105QA Gtp-Specific Succinyl-Coa Synthetase Complexed with Succinate, Magnesium Ion and Coa

Enzymatic activity of Human E105QA Gtp-Specific Succinyl-Coa Synthetase Complexed with Succinate, Magnesium Ion and Coa

All present enzymatic activity of Human E105QA Gtp-Specific Succinyl-Coa Synthetase Complexed with Succinate, Magnesium Ion and Coa:
6.2.1.4; 6.2.1.5;

Protein crystallography data

The structure of Human E105QA Gtp-Specific Succinyl-Coa Synthetase Complexed with Succinate, Magnesium Ion and Coa, PDB code: 7mss was solved by J.Huang, M.E.Fraser, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 53.01 / 1.75
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 80.471, 81.092, 54.486, 90, 103.37, 90
R / Rfree (%) 20.2 / 22.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Human E105QA Gtp-Specific Succinyl-Coa Synthetase Complexed with Succinate, Magnesium Ion and Coa (pdb code 7mss). 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 Human E105QA Gtp-Specific Succinyl-Coa Synthetase Complexed with Succinate, Magnesium Ion and Coa, PDB code: 7mss:

Magnesium binding site 1 out of 1 in 7mss

Go back to Magnesium Binding Sites List in 7mss
Magnesium binding site 1 out of 1 in the Human E105QA Gtp-Specific Succinyl-Coa Synthetase Complexed with Succinate, Magnesium Ion and Coa


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human E105QA Gtp-Specific Succinyl-Coa Synthetase Complexed with Succinate, Magnesium Ion and Coa within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg403

b:32.0
occ:1.00
 O B:HOH514 2.1 33.5 1.0
O B:HOH580 2.1 39.1 1.0
O A:HOH549 2.1 28.6 1.0
O4 A:PO4405 2.1 29.9 1.0
O B:HOH515 2.1 31.7 1.0
O3 B:SIN402 2.1 31.6 1.0
C4 B:SIN402 3.0 30.6 1.0
HA2 B:GLY272 3.3 36.8 1.0
O4 B:SIN402 3.3 30.1 1.0
H B:ALA273 3.3 30.9 1.0
P A:PO4405 3.4 29.6 1.0
H32 A:COA401 3.6 30.8 1.0
O2 A:PO4405 3.7 26.6 1.0
O1 A:PO4405 3.9 29.4 1.0
NE2 A:HIS259 4.0 29.1 1.0
HD2 A:HIS259 4.1 36.6 1.0
OD2 B:ASP295 4.1 29.6 1.0
N B:ALA273 4.1 25.6 1.0
OD1 B:ASP295 4.2 30.7 1.0
CA B:GLY272 4.3 30.5 1.0
O A:HOH607 4.4 29.3 1.0
CD2 A:HIS259 4.4 30.3 1.0
HA2 B:GLY297 4.4 41.4 1.0
OD1 A:ASN131 4.4 24.0 1.0
C3 B:SIN402 4.5 32.1 1.0
O3 A:PO4405 4.5 27.4 1.0
HB2 B:ALA273 4.6 33.5 1.0
CG B:ASP295 4.6 31.7 1.0
HB3 B:ALA273 4.6 33.5 1.0
O B:HOH631 4.7 41.4 1.0
H31 B:SIN402 4.7 38.7 1.0
HD21 A:ASN131 4.7 36.6 1.0
C3P A:COA401 4.7 25.5 1.0
HA3 B:GLY272 4.7 36.8 1.0
H B:GLY298 4.7 40.6 0.4
C B:GLY272 4.8 26.8 1.0
HG3 A:GLN105 4.8 35.4 1.0
H B:GLY272 4.8 36.5 1.0
HA3 B:GLY297 4.8 41.4 1.0
H B:GLY298 4.9 39.2 0.6
H31 A:COA401 4.9 30.8 1.0
S1P A:COA401 4.9 27.8 1.0
CB B:ALA273 5.0 27.8 1.0

Reference:

J.Huang, M.E.Fraser. The Structure of Succinyl-Coa Synthetase Bound to the Succinyl-Phosphate Intermediate Clarifies the Catalytic Mechanism of Atp-Citrate Lyase Acta Crystallogr.,Sect.F V. 78 363 2022.
ISSN: ESSN 2053-230X
DOI: 10.1107/S2053230X22008810
Page generated: Thu Oct 3 01:07:55 2024

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