Phosphorus in PDB 1a6q: Crystal Structure of the Protein Serine/Threonine Phosphatase 2C at 2 A Resolution

All present enzymatic activity of Crystal Structure of the Protein Serine/Threonine Phosphatase 2C at 2 A Resolution:
3.1.3.16;

The structure of Crystal Structure of the Protein Serine/Threonine Phosphatase 2C at 2 A Resolution, PDB code: 1a6q was solved by A.K.Das, N.R.Helps, P.T.W.Cohen, D.Barford, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	6.00 / 2.00
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	91.020, 91.020, 105.610, 90.00, 90.00, 120.00
R / Rfree (%)	21.4 / n/a

The binding sites of Phosphorus atom in the Crystal Structure of the Protein Serine/Threonine Phosphatase 2C at 2 A Resolution (pdb code 1a6q). This binding sites where shown within 5.0 Angstroms radius around Phosphorus atom.
In total only one binding site of Phosphorus was determined in the Crystal Structure of the Protein Serine/Threonine Phosphatase 2C at 2 A Resolution, PDB code: 1a6q:

Phosphorus binding site 1 out of 1 in the Crystal Structure of the Protein Serine/Threonine Phosphatase 2C at 2 A Resolution


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 1 of Crystal Structure of the Protein Serine/Threonine Phosphatase 2C at 2 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:P701 b:37.9 occ:1.00 P A:PO4701 0.0 37.9 1.0 O4 A:PO4701 1.6 41.4 1.0 O1 A:PO4701 1.6 42.5 1.0 O3 A:PO4701 1.6 45.1 1.0 O2 A:PO4701 1.7 42.0 1.0 O A:HOH702 3.4 14.6 1.0 O A:HOH802 3.5 45.7 1.0 NH1 A:ARG33 3.6 15.3 1.0 NH2 A:ARG33 3.7 18.2 1.0 O A:HOH880 3.7 17.6 1.0 O A:HOH800 3.8 31.9 1.0 CZ A:ARG33 4.1 21.5 1.0 O A:HOH799 4.2 29.8 1.0 MN A:MN384 4.2 65.6 1.0 O A:HOH776 4.3 29.0 1.0 O A:HOH741 4.7 51.4 1.0 CB A:HIS62 5.0 22.1 1.0

A.K.Das, N.R.Helps, P.T.Cohen, D.Barford. Crystal Structure of the Protein Serine/Threonine Phosphatase 2C at 2.0 A Resolution. Embo J. V. 15 6798 1996.
ISSN: ISSN 0261-4189
PubMed: 9003755