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Zinc in PDB 1kl6: Thermolysin Complexed with Z-L-Alanine (Benzyloxycarbonyl-L-Alanine)

Enzymatic activity of Thermolysin Complexed with Z-L-Alanine (Benzyloxycarbonyl-L-Alanine)

All present enzymatic activity of Thermolysin Complexed with Z-L-Alanine (Benzyloxycarbonyl-L-Alanine):
3.4.24.27;

Protein crystallography data

The structure of Thermolysin Complexed with Z-L-Alanine (Benzyloxycarbonyl-L-Alanine), PDB code: 1kl6 was solved by M.Senda, T.Senda, S.Kidokoro, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.79 / 1.80
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 93.670, 93.670, 131.477, 90.00, 90.00, 120.00
R / Rfree (%) 16.4 / 18

Other elements in 1kl6:

The structure of Thermolysin Complexed with Z-L-Alanine (Benzyloxycarbonyl-L-Alanine) also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Thermolysin Complexed with Z-L-Alanine (Benzyloxycarbonyl-L-Alanine) (pdb code 1kl6). 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 Complexed with Z-L-Alanine (Benzyloxycarbonyl-L-Alanine), PDB code: 1kl6:

Zinc binding site 1 out of 1 in 1kl6

Go back to Zinc Binding Sites List in 1kl6
Zinc binding site 1 out of 1 in the Thermolysin Complexed with Z-L-Alanine (Benzyloxycarbonyl-L-Alanine)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Thermolysin Complexed with Z-L-Alanine (Benzyloxycarbonyl-L-Alanine) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn405

b:12.1
occ:1.00
 OE2 A:GLU166 1.9 15.0 1.0
NE2 A:HIS146 2.0 11.2 1.0
O A:ALA1317 2.1 15.7 1.0
NE2 A:HIS142 2.1 12.3 1.0
C A:ALA1317 2.7 18.8 1.0
CD A:GLU166 2.8 15.5 1.0
OXT A:ALA1317 2.8 17.2 1.0
CE1 A:HIS146 2.9 12.4 1.0
OE1 A:GLU166 2.9 17.5 1.0
CD2 A:HIS142 3.0 10.8 1.0
CD2 A:HIS146 3.1 13.0 1.0
CE1 A:HIS142 3.1 12.6 1.0
OH A:TYR157 3.8 23.2 1.0
O A:HOH1411 3.9 24.8 1.0
ND1 A:HIS146 4.0 12.4 1.0
NE2 A:HIS231 4.1 16.4 1.0
CG A:HIS146 4.2 11.4 1.0
ND1 A:HIS142 4.2 10.5 1.0
CG A:HIS142 4.2 10.8 1.0
CG A:GLU166 4.2 13.5 1.0
CA A:ALA1317 4.3 17.7 1.0
CB A:SER169 4.5 11.1 1.0
CD2 A:HIS231 4.6 17.5 1.0
OG A:SER169 4.7 11.1 1.0
O A:HOH1410 4.8 15.2 1.0
CZ A:TYR157 4.8 22.4 1.0
OE2 A:GLU143 4.8 15.8 1.0
CA A:GLU166 4.9 10.6 1.0
OE1 A:GLU143 4.9 13.8 1.0
CE1 A:TYR157 5.0 23.0 1.0

Reference:

M.Senda, T.Senda, S.Kidokoro. Crystal Structure Analyses of Thermolysin in Complex with Its Inhibitors. To Be Published.
Page generated: Wed Dec 16 02:55:08 2020

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