Calcium in PDB 8tln: Structural Comparison Suggests That Thermolysin and Related Neutral Proteases Undergo Hinge-Bending Motion During Catalysis

Enzymatic activity of Structural Comparison Suggests That Thermolysin and Related Neutral Proteases Undergo Hinge-Bending Motion During Catalysis

All present enzymatic activity of Structural Comparison Suggests That Thermolysin and Related Neutral Proteases Undergo Hinge-Bending Motion During Catalysis:
3.4.24.27;

Protein crystallography data

The structure of Structural Comparison Suggests That Thermolysin and Related Neutral Proteases Undergo Hinge-Bending Motion During Catalysis, PDB code: 8tln was solved by D.Tronrud, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 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 8tln:

The structure of Structural Comparison Suggests That Thermolysin and Related Neutral Proteases Undergo Hinge-Bending Motion During Catalysis also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Structural Comparison Suggests That Thermolysin and Related Neutral Proteases Undergo Hinge-Bending Motion During Catalysis (pdb code 8tln). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the Structural Comparison Suggests That Thermolysin and Related Neutral Proteases Undergo Hinge-Bending Motion During Catalysis, PDB code: 8tln:
Jump to Calcium binding site number: 1; 2; 3; 4;

Calcium binding site 1 out of 4 in 8tln

Go back to Calcium Binding Sites List in 8tln
Calcium binding site 1 out of 4 in the Structural Comparison Suggests That Thermolysin and Related Neutral Proteases Undergo Hinge-Bending Motion During Catalysis


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structural Comparison Suggests That Thermolysin and Related Neutral Proteases Undergo Hinge-Bending Motion During Catalysis within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Ca317

b:14.9
occ:1.00
O E:GLU187 2.3 14.7 1.0
OD2 E:ASP138 2.4 15.9 1.0
OD1 E:ASP185 2.4 15.1 1.0
OE1 E:GLU190 2.5 13.8 1.0
OE1 E:GLU177 2.5 15.8 1.0
OE2 E:GLU190 2.5 16.9 1.0
O E:HOH346 2.6 13.9 1.0
CD E:GLU190 2.8 15.3 1.0
OE2 E:GLU177 2.8 15.7 1.0
CD E:GLU177 3.0 18.7 1.0
CG E:ASP138 3.3 21.7 1.0
CG E:ASP185 3.4 17.6 1.0
C E:GLU187 3.4 23.0 1.0
OD2 E:ASP185 3.7 15.5 1.0
CA E:CA318 3.8 16.4 1.0
CB E:ASP138 4.1 11.1 1.0
N E:GLU187 4.2 17.1 1.0
O E:HOH469 4.2 59.9 1.0
N E:ILE188 4.2 15.7 1.0
CG E:GLU190 4.2 15.6 1.0
OD1 E:ASP138 4.3 17.0 1.0
O E:ASP185 4.3 19.5 1.0
CA E:ILE188 4.3 12.5 1.0
CA E:GLU187 4.3 13.0 1.0
N E:GLY189 4.4 19.0 1.0
CG E:GLU177 4.5 12.4 1.0
CB E:GLU187 4.5 17.2 1.0
O E:HOH350 4.5 22.7 1.0
C E:ASP185 4.7 18.2 1.0
CB E:ASP185 4.7 19.4 1.0
N E:ASP185 4.7 16.4 1.0
C E:ILE188 4.8 22.2 1.0
N E:GLU190 4.9 13.6 1.0
O E:HOH353 4.9 18.9 1.0

Calcium binding site 2 out of 4 in 8tln

Go back to Calcium Binding Sites List in 8tln
Calcium binding site 2 out of 4 in the Structural Comparison Suggests That Thermolysin and Related Neutral Proteases Undergo Hinge-Bending Motion During Catalysis


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structural Comparison Suggests That Thermolysin and Related Neutral Proteases Undergo Hinge-Bending Motion During Catalysis within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Ca318

b:16.4
occ:1.00
OE2 E:GLU177 2.2 15.7 1.0
OD2 E:ASP185 2.3 15.5 1.0
O E:HOH475 2.3 20.6 1.0
OE2 E:GLU190 2.3 16.9 1.0
O E:HOH353 2.4 18.9 1.0
O E:ASN183 2.4 22.6 1.0
CG E:ASP185 3.2 17.6 1.0
CD E:GLU177 3.2 18.7 1.0
CD E:GLU190 3.4 15.3 1.0
C E:ASN183 3.6 21.8 1.0
OD1 E:ASP185 3.7 15.1 1.0
CG E:GLU190 3.8 15.6 1.0
OE1 E:GLU177 3.8 15.8 1.0
CA E:CA317 3.8 14.9 1.0
O E:LYS182 3.9 26.6 1.0
CA E:PRO184 4.1 17.8 1.0
CB E:ASN183 4.1 23.4 1.0
N E:ASP185 4.2 16.4 1.0
C E:PRO184 4.2 30.1 1.0
OD2 E:ASP191 4.2 18.1 1.0
CG E:GLU177 4.3 12.4 1.0
OE1 E:GLU190 4.3 13.8 1.0
N E:PRO184 4.3 20.7 1.0
OD1 E:ASP191 4.4 20.7 1.0
CB E:ASP185 4.5 19.4 1.0
O E:HOH469 4.5 59.9 1.0
CA E:ASN183 4.7 16.5 1.0
CG E:ASP191 4.7 24.0 1.0
O E:PRO184 4.8 24.3 1.0
CA E:ASP185 4.9 16.7 1.0

Calcium binding site 3 out of 4 in 8tln

Go back to Calcium Binding Sites List in 8tln
Calcium binding site 3 out of 4 in the Structural Comparison Suggests That Thermolysin and Related Neutral Proteases Undergo Hinge-Bending Motion During Catalysis


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Structural Comparison Suggests That Thermolysin and Related Neutral Proteases Undergo Hinge-Bending Motion During Catalysis within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Ca319

b:15.1
occ:1.00
O E:GLN61 2.3 15.4 1.0
OD1 E:ASP59 2.3 18.9 1.0
O E:HOH482 2.3 21.4 1.0
OD1 E:ASP57 2.3 16.4 1.0
O E:HOH503 2.4 19.1 1.0
O E:HOH419 2.4 15.6 1.0
OD2 E:ASP57 2.5 15.4 1.0
CG E:ASP57 2.8 15.3 1.0
CG E:ASP59 3.3 24.4 1.0
C E:GLN61 3.5 25.3 1.0
OD2 E:ASP59 3.8 22.9 1.0
O E:HOH484 3.9 32.6 1.0
N E:GLN61 4.0 15.5 1.0
CA E:GLN61 4.2 16.2 1.0
N E:ASP59 4.3 17.4 1.0
O E:HOH628 4.3 63.3 1.0
CB E:ASP57 4.3 9.3 1.0
CB E:GLN61 4.4 13.7 1.0
O E:HOH508 4.5 23.4 1.0
N E:PHE62 4.5 15.0 1.0
O E:HOH356 4.6 14.5 1.0
CA E:PHE62 4.6 15.0 1.0
N E:ALA58 4.6 12.7 1.0
OD2 E:ASP67 4.7 17.3 1.0
CB E:ASP59 4.7 15.1 1.0
N E:ASN60 4.8 18.4 1.0
CA E:ASP59 4.8 12.2 1.0
O E:HOH671 4.9 62.6 1.0
C E:ASP59 5.0 15.0 1.0

Calcium binding site 4 out of 4 in 8tln

Go back to Calcium Binding Sites List in 8tln
Calcium binding site 4 out of 4 in the Structural Comparison Suggests That Thermolysin and Related Neutral Proteases Undergo Hinge-Bending Motion During Catalysis


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 4 of Structural Comparison Suggests That Thermolysin and Related Neutral Proteases Undergo Hinge-Bending Motion During Catalysis within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Ca320

b:20.6
occ:1.00
O E:HOH480 2.2 32.2 1.0
OG1 E:THR194 2.2 17.8 1.0
OD1 E:ASP200 2.3 21.1 1.0
O E:ILE197 2.3 31.4 1.0
O E:THR194 2.3 17.9 1.0
O E:TYR193 2.4 18.1 1.0
O E:HOH354 2.4 18.8 1.0
C E:THR194 3.1 30.3 1.0
CG E:ASP200 3.2 19.9 1.0
CB E:THR194 3.4 19.0 1.0
C E:TYR193 3.4 23.7 1.0
C E:ILE197 3.4 44.2 1.0
CA E:THR194 3.6 16.3 1.0
OD2 E:ASP200 3.7 22.6 1.0
N E:THR194 3.9 20.0 1.0
N E:PRO195 4.1 22.3 1.0
N E:ILE197 4.2 38.1 1.0
CA E:ILE197 4.2 26.5 1.0
CB E:ILE197 4.2 33.0 1.0
O E:ASP200 4.4 19.8 1.0
N E:SER198 4.5 34.9 1.0
N E:ASP200 4.5 19.3 1.0
CG2 E:THR194 4.6 16.6 1.0
CA E:TYR193 4.6 19.1 1.0
CB E:ASP200 4.6 17.2 1.0
CA E:SER198 4.6 39.4 1.0
CA E:PRO195 4.6 25.8 1.0
CD2 E:TYR193 4.7 21.9 1.0
O E:GLU190 4.7 20.8 1.0
CB E:TYR193 4.8 26.2 1.0
C E:ASP200 4.8 12.6 1.0
C E:PRO195 4.9 38.9 1.0
C E:SER198 4.9 40.5 1.0
CG2 E:ILE197 4.9 27.1 1.0
O E:HOH476 4.9 47.7 1.0
CA E:ASP200 5.0 12.6 1.0
CG E:TYR193 5.0 20.8 1.0

Reference:

D.R.Holland, D.E.Tronrud, H.W.Pley, K.M.Flaherty, W.Stark, J.N.Jansonius, D.B.Mckay, B.W.Matthews. Structural Comparison Suggests That Thermolysin and Related Neutral Proteases Undergo Hinge-Bending Motion During Catalysis. Biochemistry V. 31 11310 1992.
ISSN: ISSN 0006-2960
PubMed: 1445869
DOI: 10.1021/BI00161A008
Page generated: Sat Dec 12 08:08:14 2020

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