Atomistry » Zinc » PDB 1kjz-1kys » 1kl6
Atomistry »
  Zinc »
    PDB 1kjz-1kys »
      1kl6 »

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

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy