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Sodium in PDB 4zvz: Co-Crystal Structures of PP5 in Complex with 5-Methyl-7- Oxabicyclo[2.2.1]Heptane-2,3-Dicarboxylic Acid

Enzymatic activity of Co-Crystal Structures of PP5 in Complex with 5-Methyl-7- Oxabicyclo[2.2.1]Heptane-2,3-Dicarboxylic Acid

All present enzymatic activity of Co-Crystal Structures of PP5 in Complex with 5-Methyl-7- Oxabicyclo[2.2.1]Heptane-2,3-Dicarboxylic Acid:
3.1.3.16;

Protein crystallography data

The structure of Co-Crystal Structures of PP5 in Complex with 5-Methyl-7- Oxabicyclo[2.2.1]Heptane-2,3-Dicarboxylic Acid, PDB code: 4zvz was solved by D.Chattopadhyay, M.R.Swingle, E.A.Salter, A.Wierzbicki, R.E.Honkanen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 91.03 / 2.00
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 40.858, 80.520, 91.165, 88.15, 87.33, 86.71
R / Rfree (%) 20.4 / 23.5

Other elements in 4zvz:

The structure of Co-Crystal Structures of PP5 in Complex with 5-Methyl-7- Oxabicyclo[2.2.1]Heptane-2,3-Dicarboxylic Acid also contains other interesting chemical elements:

Manganese (Mn) 8 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Co-Crystal Structures of PP5 in Complex with 5-Methyl-7- Oxabicyclo[2.2.1]Heptane-2,3-Dicarboxylic Acid (pdb code 4zvz). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Co-Crystal Structures of PP5 in Complex with 5-Methyl-7- Oxabicyclo[2.2.1]Heptane-2,3-Dicarboxylic Acid, PDB code: 4zvz:

Sodium binding site 1 out of 1 in 4zvz

Go back to Sodium Binding Sites List in 4zvz
Sodium binding site 1 out of 1 in the Co-Crystal Structures of PP5 in Complex with 5-Methyl-7- Oxabicyclo[2.2.1]Heptane-2,3-Dicarboxylic Acid


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Co-Crystal Structures of PP5 in Complex with 5-Methyl-7- Oxabicyclo[2.2.1]Heptane-2,3-Dicarboxylic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Na504

b:35.0
occ:1.00
ND1 C:HIS463 2.6 35.0 1.0
NE2 C:HIS474 2.7 37.9 1.0
CE1 C:HIS474 3.5 38.7 1.0
CE1 C:HIS463 3.5 34.1 1.0
CG C:HIS463 3.6 34.2 1.0
CD2 C:HIS474 3.8 36.3 1.0
OE1 C:GLN472 3.9 41.7 1.0
CB C:HIS463 3.9 35.1 1.0
ND1 C:HIS474 4.7 37.6 1.0
NE2 C:HIS463 4.7 32.5 1.0
CB C:GLN472 4.7 38.5 1.0
CD2 C:HIS463 4.8 32.5 1.0
CG C:HIS474 4.8 36.1 1.0
CD C:GLN472 4.9 41.8 1.0

Reference:

D.Chattopadhyay, M.R.Swingle, E.A.Salter, E.Wood, B.D'arcy, C.Zivanov, K.Abney, A.Musiyenko, S.F.Rusin, A.Kettenbach, L.Yet, C.E.Schroeder, J.E.Golden, W.H.Dunham, A.C.Gingras, S.Banerjee, D.Forbes, A.Wierzbicki, R.E.Honkanen. Crystal Structures and Mutagenesis of Ppp-Family Ser/Thr Protein Phosphatases Elucidate the Selectivity of Cantharidin and Novel Norcantharidin-Based Inhibitors of PP5C. Biochem. Pharmacol. V. 109 14 2016.
ISSN: ISSN 1873-2968
PubMed: 27002182
DOI: 10.1016/J.BCP.2016.03.011
Page generated: Mon Oct 7 19:46:44 2024

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