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Zinc in PDB 1kjp: Thermolysin Complexed with Z-L-Glutamic Acid (Benzyloxycarbonyl-L- Glutamic Acid)

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

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

Protein crystallography data

The structure of Thermolysin Complexed with Z-L-Glutamic Acid (Benzyloxycarbonyl-L- Glutamic Acid), PDB code: 1kjp 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) 23.44 / 1.60
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 93.745, 93.745, 131.602, 90.00, 90.00, 120.00
R / Rfree (%) 16.8 / 18

Other elements in 1kjp:

The structure of Thermolysin Complexed with Z-L-Glutamic Acid (Benzyloxycarbonyl-L- Glutamic Acid) 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-Glutamic Acid (Benzyloxycarbonyl-L- Glutamic Acid) (pdb code 1kjp). 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-Glutamic Acid (Benzyloxycarbonyl-L- Glutamic Acid), PDB code: 1kjp:

Zinc binding site 1 out of 1 in 1kjp

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


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

b:10.2
occ:1.00
 OE2 A:GLU166 1.9 11.6 1.0
NE2 A:HIS146 2.0 8.4 1.0
OXT A:GLU1317 2.0 13.5 1.0
NE2 A:HIS142 2.1 9.5 1.0
C A:GLU1317 2.7 14.1 1.0
O A:GLU1317 2.7 14.9 1.0
CD A:GLU166 2.8 13.0 1.0
CE1 A:HIS146 2.9 11.0 1.0
OE1 A:GLU166 3.0 13.5 1.0
CD2 A:HIS142 3.0 8.7 1.0
CE1 A:HIS142 3.0 9.8 1.0
CD2 A:HIS146 3.1 10.5 1.0
OH A:TYR157 3.8 17.0 1.0
O A:HOH1429 4.0 20.7 1.0
ND1 A:HIS146 4.1 10.4 1.0
ND1 A:HIS142 4.1 8.1 1.0
CA A:GLU1317 4.2 14.5 1.0
CG A:HIS142 4.2 7.8 1.0
CG A:HIS146 4.2 9.8 1.0
NE2 A:HIS231 4.2 12.3 1.0
CG A:GLU166 4.2 11.8 1.0
CB A:SER169 4.5 9.1 1.0
CD2 A:HIS231 4.7 13.3 1.0
OG A:SER169 4.7 10.4 1.0
O A:HOH1428 4.8 15.9 1.0
OE2 A:GLU143 4.8 13.0 1.0
CZ A:TYR157 4.8 16.6 1.0
CA A:GLU166 4.9 10.5 1.0
CG A:GLU1317 4.9 23.2 1.0
N A:GLU1317 4.9 15.4 1.0
CB A:GLU1317 5.0 16.4 1.0
OE1 A:GLU143 5.0 12.1 1.0
CE1 A:TYR157 5.0 15.7 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 02:54:58 2020

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