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Zinc in PDB 1fj3: Thermolysin (50% Acetone Soaked)

Enzymatic activity of Thermolysin (50% Acetone Soaked)

All present enzymatic activity of Thermolysin (50% Acetone Soaked):
3.4.24.27;

Protein crystallography data

The structure of Thermolysin (50% Acetone Soaked), PDB code: 1fj3 was solved by A.C.English, C.R.Groom, R.E.Hubbard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.00
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 94.010, 94.010, 131.030, 90.00, 90.00, 120.00
R / Rfree (%) 16 / 20.5

Other elements in 1fj3:

The structure of Thermolysin (50% Acetone Soaked) also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Thermolysin (50% Acetone Soaked) (pdb code 1fj3). 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 Thermolysin (50% Acetone Soaked), PDB code: 1fj3:

Zinc binding site 1 out of 1 in 1fj3

Go back to Zinc Binding Sites List in 1fj3
Zinc binding site 1 out of 1 in the Thermolysin (50% Acetone Soaked)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Thermolysin (50% Acetone Soaked) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn500

b:24.5
occ:1.00
NE2 A:HIS146 2.0 20.4 1.0
NE2 A:HIS142 2.0 21.0 1.0
OE1 A:GLU166 2.2 27.4 1.0
OE2 A:GLU166 2.3 30.4 1.0
O A:HOH509 2.5 43.5 1.0
CD A:GLU166 2.8 28.5 1.0
CE1 A:HIS146 3.0 21.4 1.0
CE1 A:HIS142 3.0 19.1 1.0
CD2 A:HIS146 3.1 20.0 1.0
CD2 A:HIS142 3.1 19.4 1.0
O A:HOH508 3.3 29.4 1.0
OE2 A:GLU143 3.7 27.8 1.0
ND1 A:HIS146 4.1 21.6 1.0
ND1 A:HIS142 4.1 18.3 1.0
CG A:HIS146 4.2 20.0 1.0
CG A:HIS142 4.2 18.5 1.0
CG A:GLU166 4.3 18.6 1.0
CB A:SER169 4.4 18.1 1.0
OH A:TYR157 4.4 41.8 0.4
CD A:GLU143 4.5 27.1 1.0
NE2 A:HIS231 4.5 35.6 1.0
OE1 A:GLU143 4.5 25.7 1.0
CA A:GLU166 4.6 21.2 1.0
OG A:SER169 4.7 18.5 1.0
O A:HOH591 4.8 44.1 1.0
CB A:GLU166 4.8 18.9 1.0
O A:ACN506 4.9 66.8 1.0

Reference:

A.C.English, C.R.Groom, R.E.Hubbard. Experimental and Computational Mapping of the Binding Surface of A Crystalline Protein. Protein Eng. V. 14 47 2001.
ISSN: ISSN 0269-2139
PubMed: 11287678
DOI: 10.1093/PROTEIN/14.1.47
Page generated: Wed Dec 16 02:49:12 2020

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