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Zinc in PDB 1os0: Thermolysin with An Alpha-Amino Phosphinic Inhibitor

Enzymatic activity of Thermolysin with An Alpha-Amino Phosphinic Inhibitor

All present enzymatic activity of Thermolysin with An Alpha-Amino Phosphinic Inhibitor:
3.4.24.27;

Protein crystallography data

The structure of Thermolysin with An Alpha-Amino Phosphinic Inhibitor, PDB code: 1os0 was solved by M.Selkti, A.Tomas, T.Prange, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.10
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 93.782, 93.782, 132.249, 90.00, 90.00, 120.00
R / Rfree (%) 14.6 / 17.9

Other elements in 1os0:

The structure of Thermolysin with An Alpha-Amino Phosphinic Inhibitor also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Thermolysin with An Alpha-Amino Phosphinic Inhibitor (pdb code 1os0). 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 with An Alpha-Amino Phosphinic Inhibitor, PDB code: 1os0:

Zinc binding site 1 out of 1 in 1os0

Go back to Zinc Binding Sites List in 1os0
Zinc binding site 1 out of 1 in the Thermolysin with An Alpha-Amino Phosphinic Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Thermolysin with An Alpha-Amino Phosphinic Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn600

b:8.2
occ:1.00
O1P A:0PQ605 1.9 9.9 1.0
OE2 A:GLU166 1.9 6.9 1.0
NE2 A:HIS146 2.0 4.2 1.0
NE2 A:HIS142 2.0 8.9 1.0
CD A:GLU166 2.7 7.6 1.0
CE1 A:HIS146 2.9 7.8 1.0
O2P A:0PQ605 2.9 13.3 1.0
OE1 A:GLU166 2.9 8.0 1.0
P A:0PQ605 3.0 12.3 1.0
CE1 A:HIS142 3.0 10.8 1.0
CD2 A:HIS142 3.1 10.3 1.0
CD2 A:HIS146 3.1 6.2 1.0
OH A:TYR157 3.7 13.1 1.0
NE2 A:HIS231 4.1 9.7 1.0
ND1 A:HIS146 4.1 7.5 1.0
ND1 A:HIS142 4.1 8.6 1.0
CG A:GLU166 4.2 4.7 1.0
CG A:HIS142 4.2 7.8 1.0
CM A:0PQ605 4.2 19.3 1.0
CG A:HIS146 4.2 6.3 1.0
CA1 A:0PQ605 4.2 21.1 1.0
C20 A:0PQ605 4.3 28.9 1.0
N A:0PQ605 4.4 39.3 1.0
CB A:SER169 4.6 6.2 1.0
CD2 A:HIS231 4.6 15.1 1.0
CZ A:TYR157 4.7 14.4 1.0
O A:HOH470 4.8 14.7 1.0
OG A:SER169 4.8 6.8 1.0
OE2 A:GLU143 4.9 13.1 1.0
CA A:GLU166 4.9 6.1 1.0
CE1 A:TYR157 4.9 15.8 1.0

Reference:

M.Selkti, A.Tomas, J.F.Gaucher, T.Prange, M.C.Fournie-Zaluski, H.Chen, B.P.Roques. Interactions of A New Alpha-Aminophosphinic Derivative Inside the Active Site of Tln (Thermolysin): A Model For Zinc-Metalloendopeptidase Inhibition. Acta Crystallogr.,Sect.D V. 59 1200 2003.
ISSN: ISSN 0907-4449
PubMed: 12832763
DOI: 10.1107/S0907444903010060
Page generated: Mon Jan 25 16:11:07 2021

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