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Zinc in PDB 2tmn: Crystallographic Structural Analysis of Phosphoramidates As Inhibitors and Transition-State Analogs of Thermolysin

Enzymatic activity of Crystallographic Structural Analysis of Phosphoramidates As Inhibitors and Transition-State Analogs of Thermolysin

All present enzymatic activity of Crystallographic Structural Analysis of Phosphoramidates As Inhibitors and Transition-State Analogs of Thermolysin:
3.4.24.27;

Protein crystallography data

The structure of Crystallographic Structural Analysis of Phosphoramidates As Inhibitors and Transition-State Analogs of Thermolysin, PDB code: 2tmn was solved by D.E.Tronrud, 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) N/A / 1.60
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 94.100, 94.100, 131.400, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Other elements in 2tmn:

The structure of Crystallographic Structural Analysis of Phosphoramidates As Inhibitors and Transition-State Analogs of Thermolysin also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystallographic Structural Analysis of Phosphoramidates As Inhibitors and Transition-State Analogs of Thermolysin (pdb code 2tmn). 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 Crystallographic Structural Analysis of Phosphoramidates As Inhibitors and Transition-State Analogs of Thermolysin, PDB code: 2tmn:

Zinc binding site 1 out of 1 in 2tmn

Go back to Zinc Binding Sites List in 2tmn
Zinc binding site 1 out of 1 in the Crystallographic Structural Analysis of Phosphoramidates As Inhibitors and Transition-State Analogs of Thermolysin


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystallographic Structural Analysis of Phosphoramidates As Inhibitors and Transition-State Analogs of Thermolysin within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Zn321

b:11.8
occ:1.00
 O2 E:0FA322 2.1 12.1 1.0
NE2 E:HIS146 2.1 14.4 1.0
NE2 E:HIS142 2.1 15.3 1.0
OE1 E:GLU166 2.1 15.7 1.0
O1 E:0FA322 2.8 17.4 1.0
CD E:GLU166 2.8 15.1 1.0
OE2 E:GLU166 2.9 18.6 1.0
CE1 E:HIS146 2.9 11.3 1.0
P E:0FA322 3.0 15.3 1.0
CE1 E:HIS142 3.1 9.6 1.0
CD2 E:HIS142 3.1 10.1 1.0
CD2 E:HIS146 3.2 12.5 1.0
OH E:TYR157 3.7 22.9 1.0
ND1 E:HIS146 4.1 10.7 1.0
NE2 E:HIS231 4.1 11.0 1.0
N E:0FA322 4.1 12.5 1.0
CA E:0FA322 4.2 17.4 1.0
O3 E:0FA322 4.2 14.3 1.0
CG E:HIS146 4.2 10.3 1.0
CG E:HIS142 4.3 10.3 1.0
ND1 E:HIS142 4.3 9.4 1.0
CG E:GLU166 4.3 9.2 1.0
C E:0FA322 4.5 16.8 1.0
O E:0FA322 4.6 13.7 1.0
OE1 E:GLU143 4.6 13.2 1.0
O E:HOH353 4.6 17.7 1.0
CB E:SER169 4.7 8.7 1.0
CD2 E:HIS231 4.7 12.6 1.0
CZ E:TYR157 4.7 21.5 1.0
O E:HOH490 4.8 25.7 1.0
CE2 E:TYR157 4.9 23.9 1.0
OG E:SER169 4.9 8.2 1.0
CA E:GLU166 4.9 9.3 1.0
OE2 E:GLU143 4.9 14.8 1.0

Reference:

D.E.Tronrud, A.F.Monzingo, B.W.Matthews. Crystallographic Structural Analysis of Phosphoramidates As Inhibitors and Transition-State Analogs of Thermolysin. Eur.J.Biochem. V. 157 261 1986.
ISSN: ISSN 0014-2956
PubMed: 3709536
DOI: 10.1111/J.1432-1033.1986.TB09664.X
Page generated: Thu Oct 17 03:57:33 2024

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