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Zinc in PDB 1fjq: Thermolysin (70% Acetone Soaked Crystals)

Enzymatic activity of Thermolysin (70% Acetone Soaked Crystals)

All present enzymatic activity of Thermolysin (70% Acetone Soaked Crystals):
3.4.24.27;

Protein crystallography data

The structure of Thermolysin (70% Acetone Soaked Crystals), PDB code: 1fjq 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) 1.79 / 1.70
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 94.380, 94.380, 131.710, 90.00, 90.00, 120.00
R / Rfree (%) 17 / 20.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Thermolysin (70% Acetone Soaked Crystals) (pdb code 1fjq). 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 (70% Acetone Soaked Crystals), PDB code: 1fjq:

Zinc binding site 1 out of 1 in 1fjq

Go back to Zinc Binding Sites List in 1fjq
Zinc binding site 1 out of 1 in the Thermolysin (70% Acetone Soaked Crystals)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Thermolysin (70% Acetone Soaked Crystals) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:13.2
occ:1.00
NE2 A:HIS146 2.2 12.8 1.0
O A:HOH512 2.3 37.8 1.0
NE2 A:HIS142 2.3 13.8 1.0
OE2 A:GLU166 2.6 30.3 1.0
OE1 A:GLU166 2.8 26.2 1.0
CD A:GLU166 2.9 26.7 1.0
CE1 A:HIS146 3.1 14.3 1.0
CD2 A:HIS142 3.2 14.8 1.0
CD2 A:HIS146 3.2 15.3 1.0
CE1 A:HIS142 3.2 13.6 1.0
OE2 A:GLU143 3.7 28.7 1.0
OH A:TYR157 4.1 15.1 0.4
ND1 A:HIS146 4.2 12.7 1.0
CG A:HIS146 4.2 9.4 1.0
ND1 A:HIS142 4.3 11.4 1.0
CG A:HIS142 4.3 11.8 1.0
CG A:GLU166 4.4 13.8 1.0
CB A:SER169 4.4 12.6 1.0
CD A:GLU143 4.5 20.9 1.0
OE1 A:GLU143 4.5 19.6 1.0
NE2 A:HIS231 4.5 25.3 1.0
OG A:SER169 4.7 11.4 1.0
CA A:GLU166 4.7 10.2 1.0
O A:HOH683 4.7 34.8 1.0
CB A:GLU166 4.9 10.8 1.0
CE1 A:TYR157 5.0 16.0 0.4

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: Fri Sep 25 21:34:39 2020
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