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Calcium in PDB 4oqh: Crystal Structure of Stabilized Tem-1 Beta-Lactamase Variant V.13 Carrying R164S Mutation in Complex with Boron-Based Inhibitor EC25

Protein crystallography data

The structure of Crystal Structure of Stabilized Tem-1 Beta-Lactamase Variant V.13 Carrying R164S Mutation in Complex with Boron-Based Inhibitor EC25, PDB code: 4oqh was solved by E.Dellus-Gur, M.Elias, J.S.Fraser, D.S.Tawfik, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.01 / 1.70
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 155.540, 47.030, 34.620, 90.00, 92.50, 90.00
R / Rfree (%) 18.7 / 23.3

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Stabilized Tem-1 Beta-Lactamase Variant V.13 Carrying R164S Mutation in Complex with Boron-Based Inhibitor EC25 (pdb code 4oqh). 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 Stabilized Tem-1 Beta-Lactamase Variant V.13 Carrying R164S Mutation in Complex with Boron-Based Inhibitor EC25, PDB code: 4oqh:

Calcium binding site 1 out of 1 in 4oqh

Go back to Calcium Binding Sites List in 4oqh
Calcium binding site 1 out of 1 in the Crystal Structure of Stabilized Tem-1 Beta-Lactamase Variant V.13 Carrying R164S Mutation in Complex with Boron-Based Inhibitor EC25


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 Stabilized Tem-1 Beta-Lactamase Variant V.13 Carrying R164S Mutation in Complex with Boron-Based Inhibitor EC25 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca302

b:10.1
occ:0.50
OE2 A:GLU36 2.3 5.9 1.0
O A:HOH431 2.3 14.4 1.0
O A:HOH430 2.3 11.8 1.0
CD A:GLU36 3.4 6.2 1.0
O A:HOH517 4.0 23.4 1.0
CG A:GLU36 4.0 6.2 1.0
NH2 A:ARG60 4.0 6.0 1.0
OD1 A:ASP37 4.3 18.2 1.0
OE1 A:GLU36 4.4 6.9 1.0
CB A:GLU36 4.5 7.7 1.0
CZ A:PHE59 4.6 13.0 1.0
O A:HOH479 4.7 15.7 1.0

Reference:

E.Dellus-Gur, M.Elias, E.Caselli, F.Prati, J.S.Fraser, D.S.Tawfik. Negative Epistasis in Enzyme Evolution the Thin Line Between Conformational Freedom and Anarchy To Be Published.
Page generated: Sat Dec 12 05:02:36 2020

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