Zinc 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:

Calcium (Ca) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc 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 Zinc atom.
In total only one binding site of Zinc was determined in the Structural Comparison Suggests That Thermolysin and Related Neutral Proteases Undergo Hinge-Bending Motion During Catalysis, PDB code: 8tln:

Zinc binding site 1 out of 1 in 8tln

Go back to Zinc Binding Sites List in 8tln
Zinc binding site 1 out of 1 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 Zinc with other atoms in the Zn 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:Zn321

b:16.4
occ:1.00
 OE2 E:GLU166 1.9 21.9 1.0
NE2 E:HIS142 1.9 16.1 1.0
NE2 E:HIS146 2.0 14.8 1.0
O E:HOH392 2.2 20.7 1.0
CD E:GLU166 2.6 15.3 1.0
OE1 E:GLU166 2.8 22.6 1.0
CE1 E:HIS142 2.9 13.1 1.0
CE1 E:HIS146 2.9 14.0 1.0
CD2 E:HIS146 3.0 17.3 1.0
CD2 E:HIS142 3.1 20.6 1.0
OH E:TYR157 3.7 31.0 1.0
ND1 E:HIS146 4.1 16.7 1.0
ND1 E:HIS142 4.1 10.9 1.0
CG E:GLU166 4.1 9.9 1.0
CG E:HIS146 4.1 16.0 1.0
CG E:HIS142 4.2 14.9 1.0
NE2 E:HIS231 4.3 15.6 1.0
OE1 E:GLU143 4.3 14.9 1.0
O E:HOH362 4.4 29.2 1.0
CB E:SER169 4.5 9.4 1.0
CA E:VAL1322 4.5 27.0 1.0
N E:VAL1322 4.6 24.3 1.0
OG E:SER169 4.7 14.2 1.0
CA E:GLU166 4.8 13.8 1.0
CZ E:TYR157 4.8 34.8 1.0
CD2 E:HIS231 4.8 22.2 1.0
O E:VAL1322 4.8 21.3 1.0
C E:VAL1322 4.9 68.4 1.0
CB E:GLU166 4.9 13.1 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: Thu Oct 31 11:37:54 2024

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