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Fluorine in PDB 6qdy: The Crystal Structure of Sporosarcina Pasteurii Urease in Complex with Its Substrate Urea

Enzymatic activity of The Crystal Structure of Sporosarcina Pasteurii Urease in Complex with Its Substrate Urea

All present enzymatic activity of The Crystal Structure of Sporosarcina Pasteurii Urease in Complex with Its Substrate Urea:
3.5.1.5;

Protein crystallography data

The structure of The Crystal Structure of Sporosarcina Pasteurii Urease in Complex with Its Substrate Urea, PDB code: 6qdy was solved by L.Mazzei, M.Cianci, S.Benini, S.Ciurli, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 97.54 / 1.42
Space group P 63 2 2
Cell size a, b, c (Å), α, β, γ (°) 131.565, 131.565, 188.683, 90.00, 90.00, 120.00
R / Rfree (%) 9.5 / 11.9

Other elements in 6qdy:

The structure of The Crystal Structure of Sporosarcina Pasteurii Urease in Complex with Its Substrate Urea also contains other interesting chemical elements:

Nickel (Ni) 2 atoms

Fluorine Binding Sites:

The binding sites of Fluorine atom in the The Crystal Structure of Sporosarcina Pasteurii Urease in Complex with Its Substrate Urea (pdb code 6qdy). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the The Crystal Structure of Sporosarcina Pasteurii Urease in Complex with Its Substrate Urea, PDB code: 6qdy:

Fluorine binding site 1 out of 1 in 6qdy

Go back to Fluorine Binding Sites List in 6qdy
Fluorine binding site 1 out of 1 in the The Crystal Structure of Sporosarcina Pasteurii Urease in Complex with Its Substrate Urea


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of The Crystal Structure of Sporosarcina Pasteurii Urease in Complex with Its Substrate Urea within 5.0Å range:
probe atom residue distance (Å) B Occ
C:F610

b:9.1
occ:1.00
NI C:NI601 2.0 8.9 1.0
NI C:NI602 2.1 8.3 1.0
C C:URE611 2.5 10.6 1.0
OD2 C:ASP363 2.5 9.3 1.0
O C:URE611 2.7 9.2 1.0
CE1 C:HIS137 2.8 8.1 1.0
N2 C:URE611 2.8 8.4 1.0
NE2 C:HIS137 2.8 7.5 1.0
NE2 C:HIS275 2.8 8.8 1.0
OQ2 C:KCX220 2.9 8.9 1.0
CD2 C:HIS275 2.9 8.9 1.0
N1 C:URE611 2.9 11.2 1.0
OD1 C:ASP363 3.0 8.0 1.0
OQ1 C:KCX220 3.0 8.4 1.0
CG C:ASP363 3.1 8.2 1.0
CX C:KCX220 3.3 9.0 1.0
O C:GLY280 3.9 10.3 1.0
ND1 C:HIS137 4.0 8.4 1.0
ND1 C:HIS249 4.0 7.8 1.0
CD2 C:HIS137 4.1 7.9 1.0
NE2 C:HIS139 4.1 7.8 1.0
CE1 C:HIS275 4.2 8.8 1.0
CG C:HIS275 4.2 8.4 1.0
O C:ALA366 4.3 9.5 1.0
CB C:ASP363 4.5 8.6 1.0
NZ C:KCX220 4.6 8.8 1.0
CG C:HIS137 4.7 7.9 1.0
CE1 C:HIS249 4.7 8.1 1.0
C C:GLY280 4.8 10.1 1.0
ND1 C:HIS275 4.8 8.6 1.0
CE1 C:HIS139 4.8 7.9 1.0
NE2 C:HIS222 4.9 8.5 1.0
CG2 C:THR301 4.9 8.9 1.0

Reference:

L.Mazzei, M.Cianci, S.Benini, S.Ciurli. The Structure of the Elusive Urease-Urea Complex Unveils the Mechanism of A Paradigmatic Nickel-Dependent Enzyme. Angew.Chem.Int.Ed.Engl. V. 58 7415 2019.
ISSN: ESSN 1521-3773
PubMed: 30969470
DOI: 10.1002/ANIE.201903565
Page generated: Fri Aug 2 00:46:53 2024

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