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Manganese in PDB 6asm: E. Coli Phosphoenolpyruvate Carboxykinase G209S K212C Mutant Bound to Thiosulfate

Enzymatic activity of E. Coli Phosphoenolpyruvate Carboxykinase G209S K212C Mutant Bound to Thiosulfate

All present enzymatic activity of E. Coli Phosphoenolpyruvate Carboxykinase G209S K212C Mutant Bound to Thiosulfate:
4.1.1.49;

Protein crystallography data

The structure of E. Coli Phosphoenolpyruvate Carboxykinase G209S K212C Mutant Bound to Thiosulfate, PDB code: 6asm was solved by H.Y.H.Tang, D.S.Shin, J.A.Tainer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.04 / 1.55
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 125.706, 94.080, 46.596, 90.00, 96.40, 90.00
R / Rfree (%) 17 / 18.8

Other elements in 6asm:

The structure of E. Coli Phosphoenolpyruvate Carboxykinase G209S K212C Mutant Bound to Thiosulfate also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Xenon (Xe) 1 atom

Manganese Binding Sites:

The binding sites of Manganese atom in the E. Coli Phosphoenolpyruvate Carboxykinase G209S K212C Mutant Bound to Thiosulfate (pdb code 6asm). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the E. Coli Phosphoenolpyruvate Carboxykinase G209S K212C Mutant Bound to Thiosulfate, PDB code: 6asm:

Manganese binding site 1 out of 1 in 6asm

Go back to Manganese Binding Sites List in 6asm
Manganese binding site 1 out of 1 in the E. Coli Phosphoenolpyruvate Carboxykinase G209S K212C Mutant Bound to Thiosulfate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of E. Coli Phosphoenolpyruvate Carboxykinase G209S K212C Mutant Bound to Thiosulfate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn703

b:11.3
occ:0.79
 O3G A:ATP701 2.1 16.3 0.9
OD1 A:ASP269 2.2 15.6 1.0
O A:HOH1108 2.2 17.7 1.0
NE2 A:HIS232 2.2 16.4 1.0
O A:HOH826 2.3 18.4 1.0
OD2 A:ASP269 2.6 17.1 1.0
CG A:ASP269 2.8 15.3 1.0
CE1 A:HIS232 3.2 15.0 1.0
CD2 A:HIS232 3.3 15.6 1.0
PG A:ATP701 3.3 14.0 0.9
HE1 A:HIS232 3.3 18.0 1.0
HZ1 A:LYS254 3.3 16.3 1.0
HD2 A:HIS232 3.5 18.7 1.0
HZ3 A:LYS213 3.5 24.9 1.0
HE3 A:LYS254 3.5 16.7 1.0
HE2 A:LYS213 3.6 24.0 1.0
O1G A:ATP701 3.7 14.3 1.0
HE3 A:LYS213 3.7 24.0 1.0
HE2 A:LYS254 3.8 16.7 1.0
O2G A:ATP701 3.9 14.2 1.0
CE A:LYS254 4.0 13.9 1.0
CE A:LYS213 4.0 19.9 1.0
NZ A:LYS254 4.0 13.6 1.0
O A:HOH831 4.1 15.1 1.0
HG A:SER250 4.1 26.8 1.0
NZ A:LYS213 4.2 20.7 1.0
CB A:ASP269 4.3 14.3 1.0
ND1 A:HIS232 4.3 12.9 1.0
O A:HOH1171 4.3 20.9 1.0
O A:HOH1035 4.3 23.9 1.0
O1 A:THJ706 4.4 16.8 0.6
CG A:HIS232 4.4 13.8 1.0
HZ2 A:LYS254 4.4 16.3 1.0
HE2 A:PHE413 4.5 18.6 1.0
HB2 A:ASP269 4.5 17.1 1.0
O3B A:ATP701 4.6 17.4 1.0
HZ2 A:LYS213 4.6 24.9 1.0
HZ3 A:LYS254 4.7 16.3 1.0
S2 A:THJ706 4.7 17.2 0.6
HB3 A:ASP269 4.8 17.1 1.0
HZ1 A:LYS213 4.8 24.9 1.0
HA A:ASP269 4.8 15.9 1.0
OG A:SER250 4.8 22.3 1.0
MG A:MG702 4.9 10.1 1.0
HA A:SER250 4.9 18.8 1.0
HZ A:PHE413 4.9 18.3 1.0

Reference:

H.Y.H.Tang, D.S.Shin, G.L.Hura, Y.Yang, X.Hu, F.C.Lightstone, M.D.Mcgee, H.S.Padgett, S.M.Yannone, J.A.Tainer. Structural Control of Nonnative Ligand Binding in Engineered Mutants of Phosphoenolpyruvate Carboxykinase. Biochemistry V. 57 6688 2018.
ISSN: ISSN 1520-4995
PubMed: 30376300
DOI: 10.1021/ACS.BIOCHEM.8B00963
Page generated: Tue Dec 15 04:50:40 2020

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