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Zinc in PDB 1tlp: 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: 1tlp 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) 23.30 / 2.30
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 1tlp:

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 1tlp). 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: 1tlp:

Zinc binding site 1 out of 1 in 1tlp

Go back to Zinc Binding Sites List in 1tlp
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:Zn322

b:8.4
occ:1.00
 O1P E:RDF317 1.7 5.2 1.0
OE1 E:GLU166 1.9 17.6 1.0
NE2 E:HIS146 2.2 11.3 1.0
NE2 E:HIS142 2.2 14.1 1.0
CD E:GLU166 2.6 10.9 1.0
OE2 E:GLU166 2.7 17.6 1.0
CE1 E:HIS146 3.0 3.6 1.0
P E:RDF317 3.1 16.5 1.0
CD2 E:HIS142 3.2 7.9 1.0
CE1 E:HIS142 3.2 13.7 1.0
CD2 E:HIS146 3.3 9.2 1.0
O2P E:RDF317 3.4 14.8 1.0
OH E:TYR157 3.7 27.7 1.0
N E:RDF317 4.0 24.3 1.0
NE2 E:HIS231 4.0 5.0 1.0
CA E:RDF317 4.0 14.4 1.0
CG E:GLU166 4.1 3.5 1.0
O1 E:RDF317 4.1 22.2 1.0
ND1 E:HIS146 4.2 21.8 1.0
CG E:HIS142 4.3 12.4 1.0
CG E:HIS146 4.4 5.5 1.0
ND1 E:HIS142 4.4 5.6 1.0
CD2 E:HIS231 4.5 10.9 1.0
CZ E:TYR157 4.6 30.9 1.0
CB E:SER169 4.6 1.0 1.0
C E:RDF317 4.6 11.1 1.0
OE1 E:GLU143 4.6 6.2 1.0
O E:RDF317 4.7 6.2 1.0
CE2 E:TYR157 4.7 29.0 1.0
CA E:GLU166 4.8 9.7 1.0
C1 E:RDF317 4.8 20.6 1.0
OG E:SER169 4.8 3.1 1.0
O E:HOH485 4.9 10.2 1.0
CB E:GLU166 4.9 9.1 1.0
OE2 E:GLU143 5.0 15.1 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: Wed Oct 16 19:10:47 2024

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