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Zinc in PDB 5fxn: Structure of Thermolysin Solved By Sad From Data Collected By Direct Data Collection (Ddc) Using the Esrf Robodiff Goniometer

Enzymatic activity of Structure of Thermolysin Solved By Sad From Data Collected By Direct Data Collection (Ddc) Using the Esrf Robodiff Goniometer

All present enzymatic activity of Structure of Thermolysin Solved By Sad From Data Collected By Direct Data Collection (Ddc) Using the Esrf Robodiff Goniometer:
3.4.24.27;

Protein crystallography data

The structure of Structure of Thermolysin Solved By Sad From Data Collected By Direct Data Collection (Ddc) Using the Esrf Robodiff Goniometer, PDB code: 5fxn was solved by M.W.Bowler, D.Nurizzo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 80.63 / 1.45
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 93.100, 93.100, 130.302, 90.00, 90.00, 120.00
R / Rfree (%) 14.4 / 18

Other elements in 5fxn:

The structure of Structure of Thermolysin Solved By Sad From Data Collected By Direct Data Collection (Ddc) Using the Esrf Robodiff Goniometer also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Thermolysin Solved By Sad From Data Collected By Direct Data Collection (Ddc) Using the Esrf Robodiff Goniometer (pdb code 5fxn). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Structure of Thermolysin Solved By Sad From Data Collected By Direct Data Collection (Ddc) Using the Esrf Robodiff Goniometer, PDB code: 5fxn:

Zinc binding site 1 out of 1 in 5fxn

Go back to Zinc Binding Sites List in 5fxn
Zinc binding site 1 out of 1 in the Structure of Thermolysin Solved By Sad From Data Collected By Direct Data Collection (Ddc) Using the Esrf Robodiff Goniometer


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Thermolysin Solved By Sad From Data Collected By Direct Data Collection (Ddc) Using the Esrf Robodiff Goniometer within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1317

b:15.5
occ:1.00
 NE2 A:HIS142 2.1 13.7 1.0
NE2 A:HIS146 2.1 15.8 1.0
OE2 A:GLU166 2.1 25.1 1.0
O A:HOH2172 2.2 11.3 1.0
CD A:GLU166 2.8 19.9 1.0
OE1 A:GLU166 2.9 23.1 1.0
CD2 A:HIS142 3.0 15.0 1.0
CE1 A:HIS146 3.0 16.3 1.0
CE1 A:HIS142 3.1 14.2 1.0
CD2 A:HIS146 3.1 14.6 1.0
OH A:TYR157 3.9 16.8 0.5
NE2 A:HIS231 4.1 17.9 1.0
ND1 A:HIS142 4.1 14.0 1.0
ND1 A:HIS146 4.2 16.4 1.0
CG A:HIS142 4.2 13.6 1.0
CG A:GLU166 4.2 18.2 1.0
CG A:HIS146 4.2 15.0 1.0
OE1 A:GLU143 4.3 19.3 1.0
O A:HOH2157 4.3 22.8 1.0
CA A:VAL1318 4.5 18.2 1.0
CB A:SER169 4.5 14.4 1.0
CD2 A:HIS231 4.6 18.2 1.0
N A:VAL1318 4.6 20.3 1.0
O A:VAL1318 4.7 20.4 1.0
OG A:SER169 4.7 14.4 1.0
C A:VAL1318 4.7 18.0 1.0
CA A:GLU166 4.8 14.1 1.0
CZ A:TYR157 5.0 16.2 0.5

Reference:

D.Nurizzo, M.W.Bowler, H.Caserotto, F.Dobias, T.Giraud, J.Surr, N.Guichard, G.Papp, M.Guijarro, C.Mueller-Dieckmann, D.Flot, S.Mcsweeney, F.Cipriani, P.Theveneau, G.A.Leonard. Robodiff: Combining A Sample Changer and Goniometer For Highly Automated Macromolecular Crystallography Experiments. Acta Crystallogr.,Sect.D V. 72 966 2016.
ISSN: ISSN 0907-4449
PubMed: 27487827
DOI: 10.1107/S205979831601158X
Page generated: Sun Oct 27 16:35:58 2024

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