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Chlorine in PDB 7o1b: Human Phosphomannomutase 2 (PMM2) Wild-Type Co-Crystallized with the Activator Glucose 1,6-Bisphosphate

Enzymatic activity of Human Phosphomannomutase 2 (PMM2) Wild-Type Co-Crystallized with the Activator Glucose 1,6-Bisphosphate

All present enzymatic activity of Human Phosphomannomutase 2 (PMM2) Wild-Type Co-Crystallized with the Activator Glucose 1,6-Bisphosphate:
5.4.2.8;

Protein crystallography data

The structure of Human Phosphomannomutase 2 (PMM2) Wild-Type Co-Crystallized with the Activator Glucose 1,6-Bisphosphate, PDB code: 7o1b 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) 61.45 / 3.08
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 70.96, 70.96, 364.28, 90, 90, 120
R / Rfree (%) 23.6 / 25.7

Other elements in 7o1b:

The structure of Human Phosphomannomutase 2 (PMM2) Wild-Type Co-Crystallized with the Activator Glucose 1,6-Bisphosphate also contains other interesting chemical elements:

Magnesium (Mg) 4 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Human Phosphomannomutase 2 (PMM2) Wild-Type Co-Crystallized with the Activator Glucose 1,6-Bisphosphate (pdb code 7o1b). 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) Wild-Type Co-Crystallized with the Activator Glucose 1,6-Bisphosphate, PDB code: 7o1b:

Chlorine binding site 1 out of 1 in 7o1b

Go back to Chlorine Binding Sites List in 7o1b
Chlorine binding site 1 out of 1 in the Human Phosphomannomutase 2 (PMM2) Wild-Type Co-Crystallized 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) Wild-Type Co-Crystallized with the Activator Glucose 1,6-Bisphosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl303

b:32.5
occ:1.00
 H A:PHE119 2.2 36.2 1.0
H B:PHE119 2.4 39.0 1.0
H B:ILE120 2.5 42.0 1.0
H A:ILE120 2.8 36.9 1.0
HA B:THR118 2.8 43.6 1.0
HA A:THR118 2.8 35.8 1.0
N A:PHE119 2.9 30.1 1.0
N B:PHE119 3.0 32.5 1.0
HB2 A:PHE119 3.2 34.7 1.0
HD1 A:PHE119 3.3 37.1 1.0
N B:ILE120 3.3 35.0 1.0
HB2 B:PHE119 3.4 38.9 1.0
H A:THR118 3.4 35.4 1.0
HD2 B:PHE119 3.5 38.5 1.0
CA A:THR118 3.5 29.9 1.0
CA B:THR118 3.6 36.3 1.0
N A:ILE120 3.6 30.7 1.0
C A:THR118 3.6 31.4 1.0
HB B:ILE120 3.7 44.3 1.0
H B:THR118 3.7 38.9 1.0
C B:THR118 3.8 36.9 1.0
N A:THR118 3.8 29.5 1.0
CA A:PHE119 3.8 28.0 1.0
CB A:PHE119 3.9 28.9 1.0
CA B:PHE119 3.9 32.0 1.0
N B:THR118 4.0 32.4 1.0
O B:ILE120 4.0 37.0 1.0
CB B:PHE119 4.0 32.4 1.0
CD1 A:PHE119 4.1 30.9 1.0
C B:PHE119 4.1 35.6 1.0
HG12 B:ILE120 4.1 39.4 1.0
C A:PHE119 4.2 29.1 1.0
HD13 A:ILE120 4.2 42.9 1.0
CA B:ILE120 4.3 35.9 1.0
CD2 B:PHE119 4.3 32.1 1.0
HB A:ILE120 4.3 35.6 1.0
HD12 A:ILE120 4.3 42.9 1.0
CB B:ILE120 4.3 36.9 1.0
O A:ILE120 4.4 33.5 1.0
CG A:PHE119 4.4 28.6 1.0
C B:ILE120 4.5 35.4 1.0
HG23 B:THR118 4.6 41.1 1.0
CG B:PHE119 4.7 33.1 1.0
CA A:ILE120 4.7 29.2 1.0
HA A:PHE119 4.7 33.6 1.0
CG1 B:ILE120 4.7 32.8 1.0
HB3 A:PHE119 4.7 34.7 1.0
HG23 A:THR118 4.7 38.9 1.0
CD1 A:ILE120 4.7 35.8 1.0
HA B:PHE119 4.8 38.4 1.0
O A:THR118 4.8 32.0 1.0
HD21 B:LEU104 4.8 36.1 1.0
CB B:THR118 4.8 33.9 1.0
HB3 B:PHE119 4.8 38.9 1.0
HD21 A:LEU104 4.9 32.5 1.0
C A:GLY117 4.9 30.9 1.0
CB A:THR118 4.9 29.5 1.0
C A:ILE120 4.9 30.4 1.0
HG13 B:ILE120 4.9 39.4 1.0
O B:THR118 4.9 34.8 1.0
CB A:ILE120 4.9 29.7 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: Sun Jul 13 04:39:24 2025

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