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Zinc in PDB 1esp: Neutral Protease Mutant E144S

Protein crystallography data

The structure of Neutral Protease Mutant E144S, PDB code: 1esp was solved by S.A.Litster, D.R.Wetmore, R.S.Roche, P.W.Codding, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 55.00 / 2.80
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 76.570, 76.570, 201.910, 90.00, 90.00, 120.00
R / Rfree (%) 17.8 / 22.3

Other elements in 1esp:

The structure of Neutral Protease Mutant E144S also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Neutral Protease Mutant E144S (pdb code 1esp). 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 Neutral Protease Mutant E144S, PDB code: 1esp:

Zinc binding site 1 out of 1 in 1esp

Go back to Zinc Binding Sites List in 1esp
Zinc binding site 1 out of 1 in the Neutral Protease Mutant E144S


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Neutral Protease Mutant E144S within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn323

b:23.1
occ:1.00
OE2 A:GLU167 2.0 31.6 1.0
NE2 A:HIS147 2.0 19.0 1.0
NE2 A:HIS143 2.1 14.7 1.0
O A:HOH324 2.2 23.9 1.0
CD A:GLU167 2.8 30.2 1.0
CD2 A:HIS143 2.9 12.8 1.0
OE1 A:GLU167 2.9 29.6 1.0
CE1 A:HIS147 3.0 12.2 1.0
CD2 A:HIS147 3.0 14.7 1.0
CE1 A:HIS143 3.2 14.4 1.0
ND1 A:HIS147 4.1 15.8 1.0
CG A:HIS147 4.1 12.6 1.0
CG A:HIS143 4.1 13.7 1.0
CG A:GLU167 4.2 25.6 1.0
OH A:TYR158 4.2 30.8 1.0
ND1 A:HIS143 4.3 15.3 1.0
CB A:SER170 4.7 15.8 1.0
OG A:SER170 4.7 20.3 1.0
O A:HOH328 4.8 56.3 1.0
CA A:GLU167 4.8 21.0 1.0
CE1 A:TYR158 4.8 23.6 1.0
O A:HOH337 4.8 61.5 1.0
NE2 A:HIS232 4.9 14.6 1.0
CB A:GLU167 4.9 30.6 1.0

Reference:

S.A.Lister, D.R.Wetmore, R.S.Roche, P.W.Codding. E144S Active-Site Mutant of the Bacillus Cereus Thermolysin-Like Neutral Protease at 2.8 A Resolution. Acta Crystallogr.,Sect.D V. 52 543 1996.
ISSN: ISSN 0907-4449
PubMed: 15299677
DOI: 10.1107/S0907444995016684
Page generated: Wed Dec 16 02:48:31 2020

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