Chlorine in PDB 5y2u: X-Ray Structure of Phosphoglycerate Mutase 1(PGAM1) Complexed with A Small Molecule

All present enzymatic activity of X-Ray Structure of Phosphoglycerate Mutase 1(PGAM1) Complexed with A Small Molecule:
5.4.2.11; 5.4.2.4;

The structure of X-Ray Structure of Phosphoglycerate Mutase 1(PGAM1) Complexed with A Small Molecule, PDB code: 5y2u was solved by L.L.Jiang, L.Zhou, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.54 / 1.98
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	82.640, 85.267, 102.466, 90.00, 90.00, 90.00
R / Rfree (%)	20 / 22.6

The binding sites of Chlorine atom in the X-Ray Structure of Phosphoglycerate Mutase 1(PGAM1) Complexed with A Small Molecule (pdb code 5y2u). 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 X-Ray Structure of Phosphoglycerate Mutase 1(PGAM1) Complexed with A Small Molecule, PDB code: 5y2u:

Chlorine binding site 1 out of 1 in the X-Ray Structure of Phosphoglycerate Mutase 1(PGAM1) Complexed with A Small Molecule


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of X-Ray Structure of Phosphoglycerate Mutase 1(PGAM1) Complexed with A Small Molecule within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl301 b:27.5 occ:1.00 NH2 B:ARG83 3.2 26.9 1.0 NH1 B:ARG83 3.3 28.0 1.0 NE1 B:TRP68 3.3 26.7 1.0 NH2 C:ARG83 3.3 25.6 1.0 NE1 C:TRP68 3.3 26.8 1.0 NH1 C:ARG83 3.4 26.3 1.0 CZ B:ARG83 3.7 28.0 1.0 CZ C:ARG83 3.8 25.7 1.0 CG2 C:VAL81 4.0 25.9 1.0 CB C:VAL81 4.1 27.9 1.0 CG2 B:VAL81 4.1 27.9 1.0 CB B:VAL81 4.1 27.2 1.0 CE2 B:TRP68 4.1 26.2 1.0 CD1 B:TRP68 4.1 26.9 1.0 CE2 C:TRP68 4.2 28.7 1.0 CD1 C:TRP68 4.2 22.6 1.0 CG1 C:VAL81 4.3 26.0 1.0 CG1 B:VAL81 4.3 26.8 1.0 CZ2 B:TRP68 4.4 27.1 1.0 CZ2 C:TRP68 4.5 26.5 1.0

L.Zhou, L.L.Jiang. X-Ray Structure of Phosphoglycerate Mutase 1(PGAM1) Complexed with A Small Molecule To Be Published.