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Xenon 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
Manganese (Mn) 1 atom

Xenon Binding Sites:

The binding sites of Xenon 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 Xenon atom.
In total only one binding site of Xenon was determined in the E. Coli Phosphoenolpyruvate Carboxykinase G209S K212C Mutant Bound to Thiosulfate, PDB code: 6asm:

Xenon binding site 1 out of 1 in 6asm

Go back to Xenon Binding Sites List in 6asm
Xenon 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 Xenon with other atoms in the Xe 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:Xe704

b:16.6
occ:0.64
HD23 A:LEU425 3.1 26.3 1.0
HG22 A:THR379 3.1 20.8 1.0
HG23 A:VAL426 3.2 25.6 1.0
HA A:GLN380 3.3 22.7 1.0
HG22 A:VAL426 3.4 25.6 1.0
HG A:LEU425 3.5 23.8 1.0
HG2 A:GLN380 3.5 26.7 1.0
HB2 A:PHE383 3.6 24.0 1.0
HB3 A:PHE383 3.7 24.0 1.0
HB3 A:LEU425 3.7 22.5 1.0
HD2 A:PHE383 3.7 19.9 1.0
CG2 A:VAL426 3.8 21.4 1.0
CD2 A:PHE383 3.9 16.5 1.0
CD2 A:LEU425 3.9 21.9 1.0
CB A:PHE383 3.9 20.0 1.0
CG A:PHE383 3.9 16.9 1.0
HZ A:PHE359 4.0 19.0 1.0
HA A:ALA422 4.0 21.9 1.0
CG2 A:THR379 4.0 17.3 1.0
CG A:LEU425 4.1 19.8 1.0
HD21 A:LEU425 4.1 26.3 1.0
HG3 A:GLN380 4.2 26.7 1.0
HG21 A:THR379 4.2 20.8 1.0
CA A:GLN380 4.2 18.9 1.0
O A:THR379 4.2 16.7 1.0
CG A:GLN380 4.2 22.2 1.0
HB1 A:ALA422 4.3 24.7 1.0
HG21 A:VAL426 4.3 25.6 1.0
O A:ALA422 4.4 18.0 1.0
CB A:LEU425 4.4 18.8 1.0
C A:THR379 4.4 18.0 1.0
N A:GLN380 4.4 17.5 1.0
H A:VAL426 4.4 20.0 1.0
HA A:VAL426 4.4 20.1 1.0
SD A:MET429 4.5 19.8 1.0
HG23 A:THR379 4.5 20.8 1.0
CE2 A:PHE383 4.5 16.8 1.0
N A:VAL426 4.6 16.7 1.0
HD22 A:LEU425 4.7 26.3 1.0
CD1 A:PHE383 4.7 15.3 1.0
CA A:ALA422 4.7 18.2 1.0
O A:HOH1225 4.8 15.9 1.0
CB A:GLN380 4.8 17.4 1.0
HB A:THR379 4.8 20.9 1.0
CB A:ALA422 4.9 20.5 1.0
CA A:VAL426 4.9 16.7 1.0
H A:GLN380 4.9 21.0 1.0
HE2 A:PHE383 4.9 20.1 1.0
CZ A:PHE359 4.9 15.8 1.0
C A:LEU425 4.9 16.4 1.0
CB A:VAL426 5.0 19.5 1.0
CB A:THR379 5.0 17.4 1.0
HB2 A:ALA422 5.0 24.7 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: Sun Nov 1 12:24:01 2020

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