Chlorine in PDB 7o5z: Human Phosphomannomutase 2 (PMM2) with Mutation T237M in Apo State

Enzymatic activity of Human Phosphomannomutase 2 (PMM2) with Mutation T237M in Apo State

All present enzymatic activity of Human Phosphomannomutase 2 (PMM2) with Mutation T237M in Apo State:
5.4.2.8;

Protein crystallography data

The structure of Human Phosphomannomutase 2 (PMM2) with Mutation T237M in Apo State, PDB code: 7o5z 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) 61.43 / 2.07
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 70.934, 70.934, 363.616, 90, 90, 120
R / Rfree (%) 20.4 / 22.4

Other elements in 7o5z:

The structure of Human Phosphomannomutase 2 (PMM2) with Mutation T237M in Apo State also contains other interesting chemical elements:

Magnesium (Mg) 4 atoms
Sodium (Na) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Human Phosphomannomutase 2 (PMM2) with Mutation T237M in Apo State (pdb code 7o5z). 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 Apo State, PDB code: 7o5z:

Chlorine binding site 1 out of 1 in 7o5z

Go back to Chlorine Binding Sites List in 7o5z
Chlorine binding site 1 out of 1 in the Human Phosphomannomutase 2 (PMM2) with Mutation T237M in Apo State


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 Apo State within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl1008

b:26.2
occ:1.00
 H A:PHE119 2.4 35.6 1.0
H B:PHE119 2.4 37.5 1.0
H B:ILE120 2.6 35.7 1.0
H A:ILE120 2.7 34.6 1.0
HA B:THR118 3.0 39.7 1.0
N A:PHE119 3.0 29.6 1.0
N B:PHE119 3.1 31.3 1.0
HA A:THR118 3.1 37.6 1.0
HD2 B:PHE119 3.1 37.9 1.0
HD2 A:PHE119 3.2 38.0 1.0
HB2 A:PHE119 3.2 36.7 1.0
HB2 B:PHE119 3.2 36.0 1.0
N B:ILE120 3.5 29.8 1.0
N A:ILE120 3.5 28.8 1.0
H B:THR118 3.6 41.1 1.0
H A:THR118 3.6 39.7 1.0
CA B:THR118 3.7 33.0 1.0
CA A:THR118 3.7 31.3 1.0
C A:THR118 3.8 31.7 1.0
C B:THR118 3.8 33.5 1.0
CA A:PHE119 3.8 28.3 1.0
CB A:PHE119 3.9 30.6 1.0
CA B:PHE119 3.9 33.6 1.0
CB B:PHE119 3.9 30.0 1.0
HB B:ILE120 3.9 40.5 1.0
N B:THR118 3.9 34.3 1.0
CD2 B:PHE119 3.9 31.6 1.0
N A:THR118 3.9 33.1 1.0
CD2 A:PHE119 4.0 31.6 1.0
HB A:ILE120 4.0 33.1 1.0
O A:ILE120 4.1 31.0 1.0
O B:ILE120 4.1 34.0 1.0
C B:PHE119 4.2 32.2 1.0
HG12 B:ILE120 4.2 42.0 1.0
C A:PHE119 4.2 31.7 1.0
CG A:PHE119 4.4 30.6 1.0
CG B:PHE119 4.4 33.9 1.0
CA B:ILE120 4.4 34.2 1.0
CA A:ILE120 4.5 28.2 1.0
CB B:ILE120 4.5 33.7 1.0
HD21 A:LEU104 4.6 38.1 1.0
HD21 B:LEU104 4.6 44.1 1.0
HB3 A:PHE119 4.7 36.7 1.0
HG23 B:THR118 4.7 44.3 1.0
C B:ILE120 4.7 35.7 1.0
CB A:ILE120 4.7 27.6 1.0
HG23 A:THR118 4.7 38.3 1.0
HA A:PHE119 4.7 33.9 1.0
HB3 B:PHE119 4.8 36.0 1.0
C A:ILE120 4.8 28.4 1.0
HA B:PHE119 4.8 40.4 1.0
CG1 B:ILE120 4.8 35.0 1.0
HG13 A:ILE120 4.8 37.3 1.0
O A:THR118 4.9 31.0 1.0
O B:THR118 5.0 31.0 1.0
HG13 B:ILE120 5.0 42.0 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 01:16:40 2024

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