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Calcium in PDB 3p1q: Crystal Structure of Human 14-3-3 Sigma C38N/N166H in Complex with Task-3 Peptide and Stabilizer Fusicoccin A

Protein crystallography data

The structure of Crystal Structure of Human 14-3-3 Sigma C38N/N166H in Complex with Task-3 Peptide and Stabilizer Fusicoccin A, PDB code: 3p1q was solved by C.Anders, Y.Higuchi, B.Schumacher, P.Thiel, N.Kato, C.Ottmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.57 / 1.70
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 82.460, 110.700, 62.200, 90.00, 90.00, 90.00
R / Rfree (%) 15 / 21.7

Other elements in 3p1q:

The structure of Crystal Structure of Human 14-3-3 Sigma C38N/N166H in Complex with Task-3 Peptide and Stabilizer Fusicoccin A also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms
Chlorine (Cl) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Human 14-3-3 Sigma C38N/N166H in Complex with Task-3 Peptide and Stabilizer Fusicoccin A (pdb code 3p1q). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of Human 14-3-3 Sigma C38N/N166H in Complex with Task-3 Peptide and Stabilizer Fusicoccin A, PDB code: 3p1q:

Calcium binding site 1 out of 1 in 3p1q

Go back to Calcium Binding Sites List in 3p1q
Calcium binding site 1 out of 1 in the Crystal Structure of Human 14-3-3 Sigma C38N/N166H in Complex with Task-3 Peptide and Stabilizer Fusicoccin A


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Human 14-3-3 Sigma C38N/N166H in Complex with Task-3 Peptide and Stabilizer Fusicoccin A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca253

b:33.3
occ:1.00
OG A:SER45 2.5 6.4 0.4
O13 A:FSC249 2.6 13.1 1.0
O P:HOH64 2.8 14.8 1.0
OG A:SER45 2.9 5.9 0.6
C A:SER45 3.3 8.3 1.0
N A:VAL46 3.3 6.9 1.0
CB A:SER45 3.4 7.2 0.4
O A:SER45 3.4 9.4 1.0
CD A:LYS49 3.4 12.7 0.2
CB A:SER45 3.5 6.7 0.6
C5 A:FSC249 3.5 12.1 1.0
CA A:VAL46 3.6 7.9 1.0
CD A:LYS49 3.8 15.3 0.5
C6 A:FSC249 3.8 13.1 1.0
CG2 A:VAL46 3.8 9.3 1.0
CB A:LYS49 3.9 7.4 0.2
CA A:SER45 3.9 7.6 0.4
CB A:LYS49 4.0 7.1 0.5
C2 A:FSC249 4.0 11.5 1.0
C7 A:FSC249 4.0 11.0 1.0
CA A:SER45 4.0 7.5 0.6
CB A:LYS49 4.0 6.9 0.2
NZ A:LYS49 4.1 5.3 0.2
OXT P:VAL374 4.2 15.0 1.0
C27 A:FSC249 4.3 10.9 1.0
CG A:LYS49 4.3 10.1 0.2
CB A:VAL46 4.4 7.3 1.0
CE A:LYS49 4.4 13.0 0.2
CG A:LYS49 4.4 11.1 0.5
CG A:LYS49 4.5 7.5 0.2
C12 A:FSC249 4.5 10.9 1.0
O A:HOH316 4.6 0.6 1.0
CE A:LYS49 4.6 19.4 0.5
O A:HOH265 4.6 12.8 1.0
C20 A:FSC249 4.7 12.2 1.0
C A:VAL46 4.8 8.0 1.0
O A:ASN42 4.8 9.2 1.0
C10 A:FSC249 4.9 15.0 1.0
CD A:LYS49 5.0 6.8 0.2

Reference:

C.Anders, Y.Higuchi, K.Koschinsky, M.Bartel, B.Schumacher, P.Thiel, H.Nitta, R.Preisig-Muller, G.Schlichthorl, V.Renigunta, J.Ohkanda, J.Daut, N.Kato, C.Ottmann. A Semisynthetic Fusicoccane Stabilizes A Protein-Protein Interaction and Enhances the Expression of K+ Channels at the Cell Surface Chem. Biol. V. 20 583 2013.
ISSN: ISSN 1879-1301
PubMed: 23601647
DOI: 10.1016/J.CHEMBIOL.2013.03.015
Page generated: Sat Jul 13 16:29:38 2024

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