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Zinc in PDB 3tmn: The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis

Enzymatic activity of The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis

All present enzymatic activity of The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis:
3.4.24.27;

Protein crystallography data

The structure of The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis, PDB code: 3tmn was solved by H.M.Holden, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.70
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 3tmn:

The structure of The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis (pdb code 3tmn). 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 The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis, PDB code: 3tmn:

Zinc binding site 1 out of 1 in 3tmn

Go back to Zinc Binding Sites List in 3tmn
Zinc binding site 1 out of 1 in the The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Zn323

b:17.3
occ:1.00
NE2 E:HIS146 2.1 15.8 1.0
NE2 E:HIS142 2.1 17.2 1.0
O E:HOH810 2.1 21.3 1.0
OE1 E:GLU166 2.2 15.0 1.0
OE2 E:GLU166 2.8 22.7 1.0
CD E:GLU166 2.8 18.5 1.0
CE1 E:HIS146 2.9 11.7 1.0
CE1 E:HIS142 3.1 9.3 1.0
CD2 E:HIS142 3.1 11.9 1.0
CD2 E:HIS146 3.2 17.9 1.0
OH E:TYR157 3.8 30.4 1.0
ND1 E:HIS146 4.1 12.4 1.0
NE2 E:HIS231 4.2 11.0 1.0
ND1 E:HIS142 4.2 7.6 1.0
CG E:HIS146 4.2 11.2 1.0
CG E:HIS142 4.2 9.6 1.0
OE1 E:GLU143 4.3 12.2 1.0
CG E:GLU166 4.3 10.2 1.0
CB E:SER169 4.5 6.3 1.0
O E:HOH362 4.6 27.7 1.0
CA E:VAL317 4.6 24.2 1.0
CZ E:TYR157 4.7 27.0 1.0
N E:VAL317 4.8 12.7 1.0
OG E:SER169 4.8 9.2 1.0
CD2 E:HIS231 4.8 14.7 1.0
O E:HOH807 4.8 21.9 1.0
CA E:GLU166 4.8 8.8 1.0
CE2 E:TYR157 4.9 33.1 1.0
O E:VAL317 4.9 14.5 1.0
C E:VAL317 4.9 17.2 1.0
CD E:GLU143 4.9 5.7 1.0
CB E:GLU166 4.9 10.6 1.0
OE2 E:GLU143 5.0 19.7 1.0

Reference:

H.M.Holden, B.W.Matthews. The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis. J.Biol.Chem. V. 263 3256 1988.
ISSN: ISSN 0021-9258
PubMed: 3343246
Page generated: Wed Dec 16 04:52:28 2020

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