Zinc in PDB 7tln: Structural Analysis of the Inhibition of Thermolysin By An Active- Site-Directed Irreversible Inhibitor

Enzymatic activity of Structural Analysis of the Inhibition of Thermolysin By An Active- Site-Directed Irreversible Inhibitor

All present enzymatic activity of Structural Analysis of the Inhibition of Thermolysin By An Active- Site-Directed Irreversible Inhibitor:
3.4.24.27;

Protein crystallography data

The structure of Structural Analysis of the Inhibition of Thermolysin By An Active- Site-Directed Irreversible Inhibitor, PDB code: 7tln was solved by B.W.Matthews, M.A.Holmes, D.E.Tronrud, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.30
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 94.200, 94.200, 131.400, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Other elements in 7tln:

The structure of Structural Analysis of the Inhibition of Thermolysin By An Active- Site-Directed Irreversible Inhibitor also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Structural Analysis of the Inhibition of Thermolysin By An Active- Site-Directed Irreversible Inhibitor (pdb code 7tln). 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 Structural Analysis of the Inhibition of Thermolysin By An Active- Site-Directed Irreversible Inhibitor, PDB code: 7tln:

Zinc binding site 1 out of 1 in 7tln

Go back to Zinc Binding Sites List in 7tln
Zinc binding site 1 out of 1 in the Structural Analysis of the Inhibition of Thermolysin By An Active- Site-Directed Irreversible Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structural Analysis of the Inhibition of Thermolysin By An Active- Site-Directed Irreversible Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn321

b:17.1
occ:1.00
 OE1 A:GLU166 1.9 14.3 1.0
NE2 A:HIS146 2.1 10.7 1.0
NE2 A:HIS142 2.2 16.0 1.0
OH2 A:INC322 2.5 24.5 1.0
CD A:GLU166 2.7 9.5 1.0
OE2 A:GLU166 2.7 14.0 1.0
O1 A:INC322 2.8 32.3 1.0
CE1 A:HIS146 3.0 3.5 1.0
CD2 A:HIS142 3.1 7.7 1.0
N2 A:INC322 3.1 34.5 1.0
CD2 A:HIS146 3.2 11.5 1.0
C1 A:INC322 3.2 31.5 1.0
CE1 A:HIS142 3.2 6.4 1.0
OH A:TYR157 3.8 19.6 1.0
ND1 A:HIS146 4.2 12.7 1.0
NE2 A:HIS231 4.2 8.2 1.0
CG A:GLU166 4.2 6.2 1.0
CG A:HIS142 4.2 10.1 1.0
CG A:HIS146 4.3 5.9 1.0
ND1 A:HIS142 4.3 5.2 1.0
CA2 A:INC322 4.4 24.5 1.0
OE1 A:GLU143 4.5 7.7 1.0
CB2 A:INC322 4.5 27.5 1.0
CA1 A:INC322 4.5 24.7 1.0
CB A:SER169 4.6 3.2 1.0
O A:HOH362 4.6 27.2 1.0
CD2 A:HIS231 4.7 11.0 1.0
CZ A:TYR157 4.8 26.5 1.0
O A:HOH394 4.8 49.1 1.0
CA A:GLU166 4.9 7.2 1.0
CE2 A:TYR157 4.9 21.4 1.0
OG A:SER169 4.9 4.9 1.0
CD A:GLU143 5.0 8.9 1.0

Reference:

M.A.Holmes, D.E.Tronrud, B.W.Matthews. Structural Analysis of the Inhibition of Thermolysin By An Active-Site-Directed Irreversible Inhibitor. Biochemistry V. 22 236 1983.
ISSN: ISSN 0006-2960
PubMed: 6830761
DOI: 10.1021/BI00270A034
Page generated: Wed Dec 16 14:05:04 2020

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