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Zinc in PDB 1kjo: Thermolysin Complexed with Z-L-Threonine (Benzyloxycarbonyl-L- Threonine)

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

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

Protein crystallography data

The structure of Thermolysin Complexed with Z-L-Threonine (Benzyloxycarbonyl-L- Threonine), PDB code: 1kjo 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) 26.50 / 1.60
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 93.732, 93.732, 131.581, 90.00, 90.00, 120.00
R / Rfree (%) 17.1 / 18.2

Other elements in 1kjo:

The structure of Thermolysin Complexed with Z-L-Threonine (Benzyloxycarbonyl-L- Threonine) 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-Threonine (Benzyloxycarbonyl-L- Threonine) (pdb code 1kjo). 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-Threonine (Benzyloxycarbonyl-L- Threonine), PDB code: 1kjo:

Zinc binding site 1 out of 1 in 1kjo

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


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-Threonine (Benzyloxycarbonyl-L- Threonine) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn405

b:11.5
occ:1.00
 OE2 A:GLU166 1.9 13.3 1.0
NE2 A:HIS146 2.0 10.5 1.0
O A:THR1317 2.0 13.6 1.0
NE2 A:HIS142 2.1 12.0 1.0
OXT A:THR1317 2.7 14.2 1.0
C A:THR1317 2.8 14.5 1.0
CD A:GLU166 2.8 14.2 1.0
CE1 A:HIS146 2.9 12.6 1.0
OE1 A:GLU166 3.0 15.1 1.0
CE1 A:HIS142 3.0 12.8 1.0
CD2 A:HIS142 3.0 10.7 1.0
CD2 A:HIS146 3.1 12.4 1.0
OH A:TYR157 3.8 17.8 1.0
O A:HOH1414 4.0 26.5 1.0
ND1 A:HIS146 4.1 11.4 1.0
ND1 A:HIS142 4.1 10.9 1.0
CG A:HIS142 4.2 10.3 1.0
NE2 A:HIS231 4.2 14.2 1.0
CG A:HIS146 4.2 10.8 1.0
CG A:GLU166 4.2 12.8 1.0
CA A:THR1317 4.2 14.4 1.0
CB A:SER169 4.5 10.6 1.0
CD2 A:HIS231 4.7 15.8 1.0
OG A:SER169 4.7 11.2 1.0
O A:HOH1413 4.8 16.3 1.0
CZ A:TYR157 4.8 16.6 1.0
OE2 A:GLU143 4.8 14.1 1.0
CA A:GLU166 4.9 11.0 1.0
OE1 A:GLU143 4.9 14.0 1.0
CE1 A:TYR157 5.0 17.2 1.0

Reference:

M.Senda, T.Senda, S.Kidokoro. Crystal Structure of Thermolysin in Complex with Its Inhibitors To Be Published.
Page generated: Wed Dec 16 02:54:58 2020

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