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Zinc in PDB 1tmn: Binding of N-Carboxymethyl Dipeptide Inhibitors to Thermolysin Determined By X-Ray Crystallography. A Novel Class of Transition- State Analogues For Zinc Peptidases

Enzymatic activity of Binding of N-Carboxymethyl Dipeptide Inhibitors to Thermolysin Determined By X-Ray Crystallography. A Novel Class of Transition- State Analogues For Zinc Peptidases

All present enzymatic activity of Binding of N-Carboxymethyl Dipeptide Inhibitors to Thermolysin Determined By X-Ray Crystallography. A Novel Class of Transition- State Analogues For Zinc Peptidases:
3.4.24.27;

Protein crystallography data

The structure of Binding of N-Carboxymethyl Dipeptide Inhibitors to Thermolysin Determined By X-Ray Crystallography. A Novel Class of Transition- State Analogues For Zinc Peptidases, PDB code: 1tmn was solved by A.F.Monzingo, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 14.90 / 1.90
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 (%) 17.1 / n/a

Other elements in 1tmn:

The structure of Binding of N-Carboxymethyl Dipeptide Inhibitors to Thermolysin Determined By X-Ray Crystallography. A Novel Class of Transition- State Analogues For Zinc Peptidases also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Binding of N-Carboxymethyl Dipeptide Inhibitors to Thermolysin Determined By X-Ray Crystallography. A Novel Class of Transition- State Analogues For Zinc Peptidases (pdb code 1tmn). 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 Binding of N-Carboxymethyl Dipeptide Inhibitors to Thermolysin Determined By X-Ray Crystallography. A Novel Class of Transition- State Analogues For Zinc Peptidases, PDB code: 1tmn:

Zinc binding site 1 out of 1 in 1tmn

Go back to Zinc Binding Sites List in 1tmn
Zinc binding site 1 out of 1 in the Binding of N-Carboxymethyl Dipeptide Inhibitors to Thermolysin Determined By X-Ray Crystallography. A Novel Class of Transition- State Analogues For Zinc Peptidases


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Binding of N-Carboxymethyl Dipeptide Inhibitors to Thermolysin Determined By X-Ray Crystallography. A Novel Class of Transition- State Analogues For Zinc Peptidases within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Zn322

b:14.2
occ:1.00
NE2 E:HIS142 2.0 10.7 1.0
OE1 E:GLU166 2.0 14.7 1.0
OG1 E:0ZN317 2.0 18.4 1.0
NE2 E:HIS146 2.0 11.0 1.0
OG2 E:0ZN317 2.4 21.9 1.0
CB2 E:0ZN317 2.5 22.6 1.0
CD E:GLU166 2.8 13.6 1.0
OE2 E:GLU166 2.9 15.9 1.0
CE1 E:HIS146 2.9 10.5 1.0
CD2 E:HIS142 3.0 9.2 1.0
CE1 E:HIS142 3.0 5.2 1.0
CD2 E:HIS146 3.2 6.5 1.0
OH E:TYR157 3.7 17.6 1.0
CA E:0ZN317 4.0 24.5 1.0
ND1 E:HIS146 4.1 12.5 1.0
NE2 E:HIS231 4.1 11.0 1.0
CG E:HIS142 4.1 8.2 1.0
ND1 E:HIS142 4.2 4.8 1.0
CG E:GLU166 4.2 4.3 1.0
CG E:HIS146 4.2 16.1 1.0
CB E:SER169 4.5 5.1 1.0
CA1 E:0ZN317 4.7 22.5 1.0
OE1 E:GLU143 4.7 12.3 1.0
O E:HOH362 4.7 27.7 1.0
OG E:SER169 4.7 9.5 1.0
N E:0ZN317 4.8 21.3 1.0
O E:0ZN317 4.8 17.6 1.0
CZ E:TYR157 4.8 24.5 1.0
CD2 E:HIS231 4.8 11.2 1.0
CB1 E:0ZN317 4.8 21.0 1.0
CA E:GLU166 4.8 10.4 1.0
CB E:GLU166 4.9 15.8 1.0
CE2 E:TYR157 4.9 24.5 1.0
C E:0ZN317 4.9 18.4 1.0
OE2 E:GLU143 4.9 14.8 1.0

Reference:

A.F.Monzingo, B.W.Matthews. Binding of N-Carboxymethyl Dipeptide Inhibitors to Thermolysin Determined By X-Ray Crystallography: A Novel Class of Transition-State Analogues For Zinc Peptidases Biochemistry V. 23 5724 1984.
ISSN: ISSN 0006-2960
PubMed: 6395881
DOI: 10.1021/BI00319A010
Page generated: Wed Dec 16 03:04:56 2020

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