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Fluorine in PDB 2ihz: Crystal Structure of Multifunctional Sialyltransferase From Pasteurella Multocida with Cmp-3F-NEU5AC and Alpha-Lactose Bound

Enzymatic activity of Crystal Structure of Multifunctional Sialyltransferase From Pasteurella Multocida with Cmp-3F-NEU5AC and Alpha-Lactose Bound

All present enzymatic activity of Crystal Structure of Multifunctional Sialyltransferase From Pasteurella Multocida with Cmp-3F-NEU5AC and Alpha-Lactose Bound:
2.4.99.4;

Protein crystallography data

The structure of Crystal Structure of Multifunctional Sialyltransferase From Pasteurella Multocida with Cmp-3F-NEU5AC and Alpha-Lactose Bound, PDB code: 2ihz was solved by A.J.Fisher, L.Ni, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 63.63 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 60.482, 64.532, 64.410, 90.00, 99.03, 90.00
R / Rfree (%) 21 / 25.5

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of Multifunctional Sialyltransferase From Pasteurella Multocida with Cmp-3F-NEU5AC and Alpha-Lactose Bound (pdb code 2ihz). 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 Crystal Structure of Multifunctional Sialyltransferase From Pasteurella Multocida with Cmp-3F-NEU5AC and Alpha-Lactose Bound, PDB code: 2ihz:

Fluorine binding site 1 out of 1 in 2ihz

Go back to Fluorine Binding Sites List in 2ihz
Fluorine binding site 1 out of 1 in the Crystal Structure of Multifunctional Sialyltransferase From Pasteurella Multocida with Cmp-3F-NEU5AC and Alpha-Lactose Bound


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of Multifunctional Sialyltransferase From Pasteurella Multocida with Cmp-3F-NEU5AC and Alpha-Lactose Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F1741

b:25.9
occ:1.00
 F3A A:CSF1741 0.0 25.9 1.0
C3A A:CSF1741 1.4 28.6 1.0
C2A A:CSF1741 2.4 28.6 1.0
OD2 A:ASP141 2.4 31.4 1.0
C4A A:CSF1741 2.5 28.6 1.0
C1A A:CSF1741 2.8 27.8 1.0
O6A A:CSF1741 2.8 30.1 1.0
C4 A:LBT3824 2.8 36.1 1.0
C5A A:CSF1741 2.9 29.5 1.0
C3 A:LBT3824 3.0 37.1 1.0
O3 A:LBT3824 3.1 36.6 1.0
OBA A:CSF1741 3.2 29.5 1.0
O4A A:CSF1741 3.2 22.2 1.0
CG A:ASP141 3.3 28.4 1.0
C6A A:CSF1741 3.4 31.9 1.0
OAA A:CSF1741 3.4 30.2 1.0
OD1 A:ASP141 3.4 27.6 1.0
O1A A:CSF1741 3.6 27.1 1.0
O4 A:LBT3824 3.6 34.1 1.0
C5 A:LBT3824 3.9 36.9 1.0
O7A A:CSF1741 4.2 36.2 1.0
N5A A:CSF1741 4.2 31.1 1.0
O A:HOH3843 4.3 12.7 1.0
C7A A:CSF1741 4.4 34.0 1.0
CB A:ALA35 4.5 26.1 1.0
C2 A:LBT3824 4.5 36.9 1.0
O A:ASP141 4.6 26.2 1.0
CZ2 A:TRP270 4.6 34.9 1.0
CB A:ASP141 4.7 26.3 1.0
C6 A:LBT3824 4.7 36.4 1.0
CE A:MET144 4.9 32.0 1.0
C A:ASP141 4.9 26.0 1.0
NH2 A:ARG63 5.0 33.0 1.0

Reference:

L.Ni, H.A.Chokhawala, H.Cao, R.Henning, L.Ng, S.Huang, H.Yu, X.Chen, A.J.Fisher. Crystal Structures of Pasteurella Multocida Sialyltransferase Complexes with Acceptor and Donor Analogues Reveal Substrate Binding Sites and Catalytic Mechanism. Biochemistry V. 46 6288 2007.
ISSN: ISSN 0006-2960
PubMed: 17487984
DOI: 10.1021/BI700346W
Page generated: Sun Dec 13 11:37:15 2020

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