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Zinc in PDB 3qh5: Structure of Thermolysin in Complex with N-Carbobenzyloxy-L-Aspartic Acid and L-Phenylalanine Methyl Ester

Enzymatic activity of Structure of Thermolysin in Complex with N-Carbobenzyloxy-L-Aspartic Acid and L-Phenylalanine Methyl Ester

All present enzymatic activity of Structure of Thermolysin in Complex with N-Carbobenzyloxy-L-Aspartic Acid and L-Phenylalanine Methyl Ester:
3.4.24.27;

Protein crystallography data

The structure of Structure of Thermolysin in Complex with N-Carbobenzyloxy-L-Aspartic Acid and L-Phenylalanine Methyl Ester, PDB code: 3qh5 was solved by G.Birrane, B.Bhyravbhatla, M.Navia, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.44 / 1.50
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 92.686, 92.686, 128.764, 90.00, 90.00, 120.00
R / Rfree (%) 14.4 / 18.7

Other elements in 3qh5:

The structure of Structure of Thermolysin in Complex with N-Carbobenzyloxy-L-Aspartic Acid and L-Phenylalanine Methyl Ester also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Thermolysin in Complex with N-Carbobenzyloxy-L-Aspartic Acid and L-Phenylalanine Methyl Ester (pdb code 3qh5). 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 Structure of Thermolysin in Complex with N-Carbobenzyloxy-L-Aspartic Acid and L-Phenylalanine Methyl Ester, PDB code: 3qh5:

Zinc binding site 1 out of 1 in 3qh5

Go back to Zinc Binding Sites List in 3qh5
Zinc binding site 1 out of 1 in the Structure of Thermolysin in Complex with N-Carbobenzyloxy-L-Aspartic Acid and L-Phenylalanine Methyl Ester


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Thermolysin in Complex with N-Carbobenzyloxy-L-Aspartic Acid and L-Phenylalanine Methyl Ester within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn321

b:14.3
occ:1.00
 OE1 A:GLU166 2.0 17.5 1.0
O A:NX6999 2.0 16.0 1.0
NE2 A:HIS142 2.0 13.6 1.0
NE2 A:HIS146 2.0 13.9 1.0
C A:NX6999 2.7 17.1 1.0
OXT A:NX6999 2.7 19.0 1.0
CD A:GLU166 2.7 15.0 1.0
CE1 A:HIS146 2.9 12.9 1.0
OE2 A:GLU166 2.9 15.6 1.0
CD2 A:HIS142 3.0 12.8 1.0
CE1 A:HIS142 3.0 13.4 1.0
CD2 A:HIS146 3.1 14.2 1.0
OH A:TYR157 3.8 18.5 1.0
O A:HOH491 4.1 30.7 1.0
ND1 A:HIS146 4.1 14.7 1.0
ND1 A:HIS142 4.1 13.3 1.0
CG A:HIS142 4.1 12.5 1.0
CA A:NX6999 4.1 21.7 1.0
NE2 A:HIS231 4.1 17.4 1.0
CG A:GLU166 4.2 14.6 1.0
CG A:HIS146 4.2 13.3 1.0
C1 A:PEG326 4.5 38.4 1.0
CB A:SER169 4.5 13.4 1.0
O A:HOH366 4.6 26.8 1.0
CD2 A:HIS231 4.6 17.4 1.0
OG A:SER169 4.7 12.9 1.0
OE1 A:GLU143 4.8 14.7 1.0
CA A:GLU166 4.8 12.9 1.0
CZ A:TYR157 4.9 18.5 1.0
OE2 A:GLU143 4.9 15.5 1.0
CB A:NX6999 4.9 27.9 1.0
CB A:GLU166 5.0 13.7 1.0

Reference:

G.Birrane, B.Bhyravbhatla, M.A.Navia. Synthesis of Aspartame By Thermolysin: An X-Ray Structural Study. Acs Med.Chem.Lett. V. 5 706 2014.
ISSN: ISSN 1948-5875
PubMed: 24944748
DOI: 10.1021/ML500101Z
Page generated: Sat Oct 26 12:07:03 2024

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