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

Zinc in PDB 1kro: Thermolysin Complexed with Z-D-Threonine (Benzyloxycarbonyl-D- Threonine)

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

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

Protein crystallography data

The structure of Thermolysin Complexed with Z-D-Threonine (Benzyloxycarbonyl-D- Threonine), PDB code: 1kro 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) 25.53 / 1.70
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 93.759, 93.759, 131.340, 90.00, 90.00, 120.00
R / Rfree (%) 16.6 / 18.2

Other elements in 1kro:

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

Zinc binding site 1 out of 1 in 1kro

Go back to Zinc Binding Sites List in 1kro
Zinc binding site 1 out of 1 in the Thermolysin Complexed with Z-D-Threonine (Benzyloxycarbonyl-D- 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-D-Threonine (Benzyloxycarbonyl-D- Threonine) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn405

b:11.2
occ:1.00
 OE2 A:GLU166 1.9 13.9 1.0
NE2 A:HIS146 2.0 10.2 1.0
OXT A:DTH1317 2.0 25.8 1.0
NE2 A:HIS142 2.1 11.4 1.0
O A:DTH1317 2.5 23.8 1.0
C A:DTH1317 2.6 23.6 1.0
CD A:GLU166 2.8 13.3 1.0
CE1 A:HIS146 2.9 11.7 1.0
OE1 A:GLU166 3.0 15.0 1.0
CD2 A:HIS142 3.0 11.2 1.0
CE1 A:HIS142 3.1 12.7 1.0
CD2 A:HIS146 3.1 13.2 1.0
OH A:TYR157 3.9 18.5 1.0
ND1 A:HIS146 4.1 11.2 1.0
CA A:DTH1317 4.1 23.7 1.0
ND1 A:HIS142 4.2 9.5 1.0
CG A:HIS142 4.2 9.9 1.0
CG A:HIS146 4.2 10.6 1.0
CG A:GLU166 4.2 10.9 1.0
NE2 A:HIS231 4.3 13.7 1.0
O1 A:PHQ317 4.4 26.2 1.0
CB A:SER169 4.5 10.5 1.0
O A:HOH1417 4.5 17.5 1.0
OG A:SER169 4.7 10.4 1.0
O A:HOH1418 4.7 23.7 1.0
OE1 A:GLU143 4.7 15.8 1.0
CZ A:TYR157 4.8 18.0 1.0
CD2 A:HIS231 4.8 15.5 1.0
CA A:GLU166 4.9 9.9 1.0
N A:DTH1317 4.9 24.8 1.0
CE1 A:TYR157 4.9 17.6 1.0
CG2 A:DTH1317 4.9 26.2 1.0
CB A:DTH1317 5.0 25.5 1.0
C1 A:PHQ317 5.0 25.4 1.0

Reference:

M.Senda, T.Senda, S.Kidokoro. Crystal Structure Analyses of Thermolysin in Complex with Its Inhibitors. To Be Published.
Page generated: Sun Oct 13 04:39:24 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy