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Zinc in PDB 1gxw: The 2.2 A Resolution Structure of Thermolysin Crystallized in Presence of Potassium Thiocyanate

Enzymatic activity of The 2.2 A Resolution Structure of Thermolysin Crystallized in Presence of Potassium Thiocyanate

All present enzymatic activity of The 2.2 A Resolution Structure of Thermolysin Crystallized in Presence of Potassium Thiocyanate:
3.4.24.27;

Protein crystallography data

The structure of The 2.2 A Resolution Structure of Thermolysin Crystallized in Presence of Potassium Thiocyanate, PDB code: 1gxw was solved by J.F.Gaucher, M.Selkti, T.Prange, A.Tomas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 18.46 / 2.18
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 93.170, 93.170, 130.630, 90.00, 90.00, 120.00
R / Rfree (%) 16.3 / 21.5

Other elements in 1gxw:

The structure of The 2.2 A Resolution Structure of Thermolysin Crystallized in Presence of Potassium Thiocyanate also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the The 2.2 A Resolution Structure of Thermolysin Crystallized in Presence of Potassium Thiocyanate (pdb code 1gxw). 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 The 2.2 A Resolution Structure of Thermolysin Crystallized in Presence of Potassium Thiocyanate, PDB code: 1gxw:

Zinc binding site 1 out of 1 in 1gxw

Go back to Zinc Binding Sites List in 1gxw
Zinc binding site 1 out of 1 in the The 2.2 A Resolution Structure of Thermolysin Crystallized in Presence of Potassium Thiocyanate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The 2.2 A Resolution Structure of Thermolysin Crystallized in Presence of Potassium Thiocyanate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1321

b:15.8
occ:1.00
 NE2 A:HIS146 2.1 6.8 1.0
OE1 A:GLU166 2.2 11.0 1.0
NE2 A:HIS142 2.2 11.8 1.0
CE1 A:HIS146 3.0 9.2 1.0
CD A:GLU166 3.0 16.9 1.0
CD2 A:HIS142 3.1 11.3 1.0
S A:SCN1322 3.1 16.1 1.0
OE2 A:GLU166 3.2 24.1 1.0
CD2 A:HIS146 3.2 8.6 1.0
CE1 A:HIS142 3.2 10.6 1.0
ND1 A:HIS146 4.1 8.1 1.0
C A:SCN1322 4.2 25.1 1.0
CG A:HIS146 4.3 10.8 1.0
CG A:HIS142 4.3 10.8 1.0
ND1 A:HIS142 4.3 11.2 1.0
O A:HOH2089 4.3 23.6 1.0
CG A:GLU166 4.4 14.6 1.0
OE1 A:GLU143 4.5 10.0 1.0
CA A:VAL322 4.5 21.8 1.0
CB A:SER169 4.5 6.1 1.0
NE2 A:HIS231 4.6 15.0 1.0
O A:VAL322 4.6 20.1 1.0
OG A:SER169 4.7 7.3 1.0
C A:VAL322 4.7 21.1 1.0
CD2 A:HIS231 4.7 17.8 1.0
CA A:GLU166 4.7 11.1 1.0
CB A:GLU166 4.9 11.7 1.0
OE2 A:GLU143 4.9 13.7 1.0
N A:VAL322 4.9 22.1 1.0

Reference:

J.Gaucher, M.Selkti, T.Prange, A.Tomas. The 2.2 A Resolution Structure of Thermolysin (Tln) Crystallized in the Presence of Potassium Thiocyanate. Acta Crystallogr.,Sect.D V. 58 2198 2002.
ISSN: ISSN 0907-4449
PubMed: 12454500
DOI: 10.1107/S0907444902015457
Page generated: Sun Oct 13 01:48:41 2024

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