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Sodium in PDB 5cgx: Crystal Structure of Fox-4 Cephamycinase Mutant Y150F Complexed with Cefoxitin

Enzymatic activity of Crystal Structure of Fox-4 Cephamycinase Mutant Y150F Complexed with Cefoxitin

All present enzymatic activity of Crystal Structure of Fox-4 Cephamycinase Mutant Y150F Complexed with Cefoxitin:
3.5.2.6;

Protein crystallography data

The structure of Crystal Structure of Fox-4 Cephamycinase Mutant Y150F Complexed with Cefoxitin, PDB code: 5cgx was solved by V.N.Malashkevich, R.Toro, S.Lefurgy, S.C.Almo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.64 / 1.21
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 54.524, 56.588, 55.485, 90.00, 99.23, 90.00
R / Rfree (%) 18.1 / 20.5

Other elements in 5cgx:

The structure of Crystal Structure of Fox-4 Cephamycinase Mutant Y150F Complexed with Cefoxitin also contains other interesting chemical elements:

Zinc (Zn) 6 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Fox-4 Cephamycinase Mutant Y150F Complexed with Cefoxitin (pdb code 5cgx). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of Fox-4 Cephamycinase Mutant Y150F Complexed with Cefoxitin, PDB code: 5cgx:

Sodium binding site 1 out of 1 in 5cgx

Go back to Sodium Binding Sites List in 5cgx
Sodium binding site 1 out of 1 in the Crystal Structure of Fox-4 Cephamycinase Mutant Y150F Complexed with Cefoxitin


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Fox-4 Cephamycinase Mutant Y150F Complexed with Cefoxitin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na407

b:16.5
occ:1.00
 ND1 A:HIS160 2.3 19.2 1.0
OE2 A:GLU220 2.3 13.0 1.0
O A:HOH751 2.4 20.1 1.0
CE1 A:HIS160 3.1 22.8 1.0
HE1 A:HIS160 3.2 27.4 1.0
HD22 A:LEU217 3.3 15.8 1.0
CD A:GLU220 3.3 12.7 1.0
CG A:HIS160 3.3 14.1 1.0
HB2 A:HIS160 3.3 14.1 1.0
HA A:HIS160 3.5 11.9 1.0
HD23 A:LEU217 3.5 15.8 1.0
HB3 A:PHE170 3.5 17.1 1.0
OE1 A:GLU220 3.7 11.8 1.0
CD2 A:LEU217 3.7 13.2 1.0
HB2 A:PHE170 3.7 17.1 1.0
CB A:HIS160 3.7 11.7 1.0
HD21 A:LEU217 3.8 15.8 1.0
O A:HOH753 3.9 18.8 1.0
CB A:PHE170 4.1 14.3 1.0
CA A:HIS160 4.1 9.9 1.0
H A:PHE170 4.1 17.3 1.0
NE2 A:HIS160 4.3 25.6 1.0
CD2 A:HIS160 4.4 23.4 1.0
HA A:LEU217 4.6 13.1 1.0
O A:HOH641 4.6 33.3 1.0
HB3 A:HIS160 4.6 14.1 1.0
CG A:GLU220 4.7 11.3 1.0
O A:HOH652 4.7 30.9 1.0
HG2 A:GLU220 4.7 13.5 1.0
N A:PHE170 4.9 14.4 1.0
CG A:PHE170 5.0 11.9 1.0
HG3 A:GLU220 5.0 13.5 1.0

Reference:

S.T.Lefurgy, V.N.Malashkevich, J.T.Aguilan, E.Nieves, E.C.Mundorff, B.Biju, M.A.Noel, R.Toro, D.Baiwir, K.M.Papp-Wallace, S.C.Almo, J.M.Frere, G.Bou, R.A.Bonomo. Fox-4 Cephamycinase: An Analysis of Structure and Function. Antimicrob.Agents Chemother. 2015.
ISSN: ESSN 1098-6596
PubMed: 26525784
DOI: 10.1128/AAC.01887-15
Page generated: Mon Oct 7 20:20:16 2024

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