Chlorine in PDB 7o58: Human Phosphomannomutase 2 (PMM2) with Mutation T237M in Complex with the Activator Glucose 1,6-Bisphosphate

Enzymatic activity of Human Phosphomannomutase 2 (PMM2) with Mutation T237M in Complex with the Activator Glucose 1,6-Bisphosphate

All present enzymatic activity of Human Phosphomannomutase 2 (PMM2) with Mutation T237M in Complex with the Activator Glucose 1,6-Bisphosphate:
5.4.2.8;

Protein crystallography data

The structure of Human Phosphomannomutase 2 (PMM2) with Mutation T237M in Complex with the Activator Glucose 1,6-Bisphosphate, PDB code: 7o58 was solved by S.Ramon-Maiques, A.Briso-Montiano, F.Del Cano-Ochoa, A.Vilas, B.Perez, V.Rubio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 59.95 / 1.97
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 70.52, 70.52, 359.72, 90, 90, 120
R / Rfree (%) 18.3 / 23

Other elements in 7o58:

The structure of Human Phosphomannomutase 2 (PMM2) with Mutation T237M in Complex with the Activator Glucose 1,6-Bisphosphate also contains other interesting chemical elements:

Sodium (Na) 3 atoms
Magnesium (Mg) 4 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Human Phosphomannomutase 2 (PMM2) with Mutation T237M in Complex with the Activator Glucose 1,6-Bisphosphate (pdb code 7o58). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Human Phosphomannomutase 2 (PMM2) with Mutation T237M in Complex with the Activator Glucose 1,6-Bisphosphate, PDB code: 7o58:

Chlorine binding site 1 out of 1 in 7o58

Go back to Chlorine Binding Sites List in 7o58
Chlorine binding site 1 out of 1 in the Human Phosphomannomutase 2 (PMM2) with Mutation T237M in Complex with the Activator Glucose 1,6-Bisphosphate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human Phosphomannomutase 2 (PMM2) with Mutation T237M in Complex with the Activator Glucose 1,6-Bisphosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl409

b:34.4
occ:1.00
 H B:PHE119 2.4 45.2 1.0
H A:PHE119 2.4 41.3 1.0
H B:ILE120 2.7 41.7 1.0
H A:ILE120 2.7 42.2 1.0
HA B:THR118 3.0 41.5 1.0
HD2 A:PHE119 3.0 39.4 1.0
HA A:THR118 3.0 39.9 1.0
N A:PHE119 3.0 34.4 1.0
N B:PHE119 3.1 37.6 1.0
HB2 A:PHE119 3.1 42.5 1.0
HD2 B:PHE119 3.1 48.5 1.0
HB2 B:PHE119 3.2 40.7 1.0
N B:ILE120 3.5 34.7 1.0
H A:THR118 3.5 42.4 1.0
N A:ILE120 3.5 35.2 1.0
H B:THR118 3.6 45.9 1.0
CA A:THR118 3.7 33.2 1.0
CA B:THR118 3.7 34.6 1.0
C A:THR118 3.8 35.0 1.0
CB A:PHE119 3.8 35.4 1.0
CA A:PHE119 3.8 36.2 1.0
C B:THR118 3.8 38.0 1.0
CD2 A:PHE119 3.8 32.9 1.0
CA B:PHE119 3.9 38.3 1.0
CB B:PHE119 3.9 33.9 1.0
N A:THR118 3.9 35.3 1.0
CD2 B:PHE119 3.9 40.4 1.0
N B:THR118 3.9 38.3 1.0
HB B:ILE120 4.0 51.3 1.0
HB A:ILE120 4.0 40.9 1.0
O B:ILE120 4.1 35.2 1.0
C A:PHE119 4.2 37.2 1.0
C B:PHE119 4.2 38.2 1.0
O A:ILE120 4.2 37.2 1.0
CG A:PHE119 4.3 31.3 1.0
CG B:PHE119 4.4 41.0 1.0
CA B:ILE120 4.5 39.3 1.0
CA A:ILE120 4.5 30.2 1.0
HG13 A:ILE120 4.5 51.6 1.0
HD21 A:LEU104 4.5 40.3 1.0
HD21 B:LEU104 4.6 47.0 1.0
HB3 A:PHE119 4.6 42.5 1.0
CB B:ILE120 4.6 42.7 1.0
CB A:ILE120 4.7 34.1 1.0
HG13 B:ILE120 4.7 50.5 1.0
HB3 B:PHE119 4.7 40.7 1.0
C B:ILE120 4.7 35.4 1.0
HA A:PHE119 4.7 43.5 1.0
HA B:PHE119 4.8 45.9 1.0
C A:ILE120 4.8 36.7 1.0
HG23 B:THR118 4.9 51.8 1.0
HD23 A:LEU104 4.9 40.3 1.0
CE2 A:PHE119 4.9 34.6 1.0
O A:THR118 4.9 36.3 1.0
O B:THR118 5.0 36.4 1.0
HG23 A:THR118 5.0 41.3 1.0
HE2 A:PHE119 5.0 41.5 1.0

Reference:

A.Briso-Montiano, F.Del Cano-Ochoa, A.Vilas, A.Velazquez-Campoy, V.Rubio, B.Perez, S.Ramon-Maiques. Insight on Molecular Pathogenesis and Pharmacochaperoning Potential in Phosphomannomutase 2 Deficiency, Provided By Novel Human Phosphomannomutase 2 Structures. J Inherit Metab Dis V. 45 318 2022.
ISSN: ISSN 1573-2665
PubMed: 34859900
DOI: 10.1002/JIMD.12461
Page generated: Tue Jul 30 01:14:45 2024

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