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

Enzymatic activity of 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;

Protein crystallography data

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

Manganese Binding Sites:

The binding sites of Manganese 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 Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of the Protein Serine/Threonine Phosphatase 2C at 2 A Resolution, PDB code: 1a6q:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 1a6q

Go back to Manganese Binding Sites List in 1a6q
Manganese binding site 1 out of 2 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 Manganese with other atoms in the Mn 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:Mn383

b:34.1
occ:1.00
O A:HOH799 1.7 29.8 1.0
O A:HOH889 1.9 29.6 1.0
OD2 A:ASP282 2.2 23.2 1.0
O A:HOH880 2.2 17.6 1.0
OD2 A:ASP60 2.2 15.3 1.0
OD1 A:ASP239 2.3 21.4 1.0
CG A:ASP60 3.0 16.0 1.0
CG A:ASP282 3.1 20.7 1.0
OD1 A:ASP60 3.2 24.6 1.0
CG A:ASP239 3.3 16.2 1.0
OD1 A:ASP282 3.4 23.4 1.0
OD2 A:ASP239 3.5 18.7 1.0
O1 A:PO4701 3.7 42.5 1.0
O A:HOH702 3.8 14.6 1.0
MN A:MN384 4.0 65.6 1.0
O A:HOH749 4.1 28.4 1.0
O A:HOH885 4.2 22.5 1.0
O A:HOH883 4.3 18.6 1.0
N A:GLY240 4.4 10.5 1.0
CB A:ASP60 4.4 18.1 1.0
O A:HOH879 4.4 28.2 1.0
CB A:ASP282 4.5 15.9 1.0
O A:ASN283 4.6 16.1 1.0
CB A:ASP239 4.7 12.6 1.0
N A:ASP239 4.8 8.3 1.0
OD1 A:ASP38 4.8 12.4 1.0
CB A:CYS238 4.9 11.6 1.0
C A:ASP239 4.9 12.8 1.0
SG A:CYS238 4.9 17.9 1.0
O A:HOH881 5.0 10.6 1.0
CA A:GLY240 5.0 11.7 1.0

Manganese binding site 2 out of 2 in 1a6q

Go back to Manganese Binding Sites List in 1a6q
Manganese binding site 2 out of 2 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 Manganese with other atoms in the Mn binding site number 2 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:Mn384

b:65.6
occ:1.00
O A:HOH702 2.1 14.6 1.0
O A:GLY61 2.1 17.1 1.0
O A:HOH880 2.3 17.6 1.0
O A:HOH800 2.3 31.9 1.0
OD1 A:ASP60 2.5 24.6 1.0
O A:HOH879 2.6 28.2 1.0
C A:GLY61 3.3 17.8 1.0
CG A:ASP60 3.7 16.0 1.0
OE1 A:GLU37 3.8 23.1 1.0
O3 A:PO4701 3.9 45.1 1.0
O1 A:PO4701 3.9 42.5 1.0
MN A:MN383 4.0 34.1 1.0
CA A:HIS62 4.0 18.1 1.0
O4 A:PO4701 4.0 41.4 1.0
O A:HOH881 4.1 10.6 1.0
N A:HIS62 4.1 17.5 1.0
CB A:GLU37 4.1 20.7 1.0
N A:GLY61 4.2 14.5 1.0
O A:HOH889 4.2 29.6 1.0
O A:HOH799 4.2 29.8 1.0
P A:PO4701 4.2 37.9 1.0
OD2 A:ASP60 4.2 15.3 1.0
CB A:HIS62 4.3 22.1 1.0
C A:ASP60 4.3 15.0 1.0
CA A:GLY61 4.3 17.6 1.0
O A:HOH882 4.3 26.7 1.0
OD1 A:ASN283 4.5 10.3 1.0
O A:ASP60 4.5 13.3 1.0
OD1 A:ASP38 4.6 12.4 1.0
OD1 A:ASP282 4.6 23.4 1.0
CD A:GLU37 4.8 24.1 1.0
CB A:ASP60 4.9 18.1 1.0
CA A:ASP60 4.9 16.3 1.0
O A:HOH776 4.9 29.0 1.0

Reference:

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
Page generated: Tue Dec 15 03:46:04 2020

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