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Sodium in PDB 4cg0: Savinase Crystal Structures For Combined Single Crystal Diffraction and Powder Diffraction Analysis

Enzymatic activity of Savinase Crystal Structures For Combined Single Crystal Diffraction and Powder Diffraction Analysis

All present enzymatic activity of Savinase Crystal Structures For Combined Single Crystal Diffraction and Powder Diffraction Analysis:
3.4.21.62;

Protein crystallography data

The structure of Savinase Crystal Structures For Combined Single Crystal Diffraction and Powder Diffraction Analysis, PDB code: 4cg0 was solved by C.G.Frankaer, O.V.Moroz, J.P.Turkenburg, S.I.Aspmo, M.Thymark, E.P.Friis, K.Stahla, J.E.Nielsen, K.S.Wilson, P.Harris, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.80 / 1.36
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 53.040, 57.550, 71.370, 90.00, 90.00, 90.00
R / Rfree (%) 10.908 / 15.413

Other elements in 4cg0:

The structure of Savinase Crystal Structures For Combined Single Crystal Diffraction and Powder Diffraction Analysis also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Savinase Crystal Structures For Combined Single Crystal Diffraction and Powder Diffraction Analysis (pdb code 4cg0). 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 Savinase Crystal Structures For Combined Single Crystal Diffraction and Powder Diffraction Analysis, PDB code: 4cg0:

Sodium binding site 1 out of 1 in 4cg0

Go back to Sodium Binding Sites List in 4cg0
Sodium binding site 1 out of 1 in the Savinase Crystal Structures For Combined Single Crystal Diffraction and Powder Diffraction Analysis


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Savinase Crystal Structures For Combined Single Crystal Diffraction and Powder Diffraction Analysis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na302

b:11.8
occ:1.00
 O A:ALA168 2.2 11.7 1.0
O A:TYR165 2.3 11.6 1.0
O A:ALA163 2.3 11.0 1.0
O A:HOH2266 2.3 20.0 1.0
O A:HOH2259 2.4 16.6 1.0
C A:TYR165 3.3 10.2 1.0
C A:ALA168 3.4 11.0 1.0
C A:ALA163 3.5 10.0 1.0
C A:ARG164 3.9 11.4 1.0
O A:ALA166 3.9 12.9 1.0
N A:TYR165 4.0 10.5 1.0
CA A:ALA166 4.0 13.3 1.0
N A:ALA168 4.0 10.9 1.0
C A:ALA166 4.0 10.8 1.0
O A:ARG164 4.0 14.9 1.0
N A:ALA166 4.0 12.2 1.0
CA A:ALA168 4.0 10.3 1.0
O A:GLY189 4.1 13.2 1.0
CB A:ALA168 4.2 12.2 1.0
OD2 A:ASP191 4.2 20.5 1.0
CA A:TYR165 4.2 11.7 1.0
CA A:ARG164 4.3 12.4 1.0
CB A:ALA170 4.3 10.4 1.0
N A:ARG164 4.3 10.5 1.0
NH2 A:ARG241 4.3 18.0 1.0
N A:ALA170 4.3 8.8 1.0
N A:MET169 4.4 10.2 1.0
CA A:ALA163 4.5 10.9 1.0
CA A:MET169 4.7 10.2 1.0
N A:ASN167 4.8 11.4 1.0
O A:PRO162 4.8 10.6 1.0
O A:HOH2293 4.8 34.2 1.0
C A:MET169 4.9 9.7 1.0
CA A:ALA170 4.9 10.0 1.0

Reference:

C.G.Frankaer, O.V.Moroz, J.P.Turkenburg, S.I.Aspmo, M.Thymark, E.P.Friis, K.Stahl, J.E.Nielsen, K.S.Wilson, P.Harris. Analysis of An Industrial Production Suspension of Bacillus Lentus Subtilisin Crystals By Powder Diffraction: A Powerful Quality-Control Tool. Acta Crystallogr.,Sect.D V. 70 1115 2014.
ISSN: ISSN 0907-4449
PubMed: 24699655
DOI: 10.1107/S1399004714001497
Page generated: Mon Oct 7 14:43:34 2024

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