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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

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