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Zinc in PDB 4d9w: Thermolysin in Complex with UBTLN32

Enzymatic activity of Thermolysin in Complex with UBTLN32

All present enzymatic activity of Thermolysin in Complex with UBTLN32:
3.4.24.27;

Protein crystallography data

The structure of Thermolysin in Complex with UBTLN32, PDB code: 4d9w was solved by A.Biela, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 22.30 / 1.38
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 93.100, 93.100, 130.900, 90.00, 90.00, 120.00
R / Rfree (%) 10.9 / 14

Other elements in 4d9w:

The structure of Thermolysin in Complex with UBTLN32 also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Thermolysin in Complex with UBTLN32 (pdb code 4d9w). 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 in Complex with UBTLN32, PDB code: 4d9w:

Zinc binding site 1 out of 1 in 4d9w

Go back to Zinc Binding Sites List in 4d9w
Zinc binding site 1 out of 1 in the Thermolysin in Complex with UBTLN32


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Thermolysin in Complex with UBTLN32 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn408

b:6.9
occ:1.00
OE2 A:GLU166 2.0 8.2 1.0
O24 A:X32401 2.0 6.8 1.0
NE2 A:HIS146 2.0 7.0 1.0
NE2 A:HIS142 2.0 6.5 1.0
CD A:GLU166 2.8 7.3 1.0
CE1 A:HIS146 2.9 7.5 1.0
OE1 A:GLU166 3.0 7.9 1.0
HE1 A:HIS146 3.0 9.0 1.0
P12 A:X32401 3.0 7.2 1.0
CE1 A:HIS142 3.0 6.6 1.0
CD2 A:HIS142 3.0 6.5 1.0
O23 A:X32401 3.1 8.1 1.0
CD2 A:HIS146 3.1 6.9 1.0
HH A:TYR157 3.2 12.3 1.0
HE1 A:HIS142 3.2 8.0 1.0
HD2 A:HIS142 3.2 7.8 1.0
HE2 A:HIS231 3.3 10.6 1.0
HD2 A:HIS146 3.4 8.3 1.0
OH A:TYR157 3.8 10.2 1.0
NE2 A:HIS231 4.0 8.8 1.0
HA A:GLU166 4.0 7.5 1.0
N13 A:X32401 4.1 8.4 1.0
ND1 A:HIS146 4.1 7.6 1.0
HB2 A:SER169 4.1 7.5 1.0
ND1 A:HIS142 4.1 6.5 1.0
HG A:SER169 4.1 7.8 1.0
C14 A:X32401 4.1 8.0 1.0
CG A:HIS142 4.2 6.2 1.0
CG A:HIS146 4.2 6.7 1.0
CG A:GLU166 4.2 7.6 1.0
HB3 A:SER169 4.3 7.5 1.0
HD2 A:HIS231 4.4 10.6 1.0
HE1 A:TYR157 4.4 11.0 1.0
HG2 A:GLU166 4.4 9.2 1.0
C11 A:X32401 4.5 10.9 1.0
CD2 A:HIS231 4.5 8.8 1.0
CB A:SER169 4.6 6.2 1.0
C15 A:X32401 4.6 8.3 1.0
N10 A:X32401 4.6 13.0 0.6
O29 A:X32401 4.6 9.1 1.0
C3 A:GOL402 4.6 14.6 1.0
N10 A:X32401 4.7 13.1 0.4
HG3 A:GLU166 4.7 9.2 1.0
OG A:SER169 4.8 6.5 1.0
O3 A:GOL402 4.8 9.3 1.0
HD1 A:HIS146 4.8 9.1 1.0
CZ A:TYR157 4.8 9.3 1.0
OE1 A:GLU143 4.8 10.9 1.0
HH22 A:ARG203 4.8 9.4 1.0
HD1 A:HIS142 4.9 7.7 1.0
CA A:GLU166 4.9 6.2 1.0
CE1 A:TYR157 4.9 9.2 1.0

Reference:

A.Biela, N.Nasief, A.Heine, D.Hangauer, G.Klebe. Thermolysin Inhibition To Be Published.
Page generated: Wed Dec 16 05:10:53 2020

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