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Sodium in PDB 6ru1: Crystal Structure of Glucuronoyl Esterase From Cerrena Unicolor Inactive S270A Variant in Complex with the Aldouronic Acid UM4X

Protein crystallography data

The structure of Crystal Structure of Glucuronoyl Esterase From Cerrena Unicolor Inactive S270A Variant in Complex with the Aldouronic Acid UM4X, PDB code: 6ru1 was solved by H.A.Ernst, C.Mosbech, A.Langkilde, P.Westh, A.Meyer, J.W.Agger, S.Larsen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.12 / 1.39
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 84.240, 84.240, 260.815, 90.00, 90.00, 90.00
R / Rfree (%) 16.3 / 17.7

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Glucuronoyl Esterase From Cerrena Unicolor Inactive S270A Variant in Complex with the Aldouronic Acid UM4X (pdb code 6ru1). 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 Glucuronoyl Esterase From Cerrena Unicolor Inactive S270A Variant in Complex with the Aldouronic Acid UM4X, PDB code: 6ru1:

Sodium binding site 1 out of 1 in 6ru1

Go back to Sodium Binding Sites List in 6ru1
Sodium binding site 1 out of 1 in the Crystal Structure of Glucuronoyl Esterase From Cerrena Unicolor Inactive S270A Variant in Complex with the Aldouronic Acid UM4X


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 Glucuronoyl Esterase From Cerrena Unicolor Inactive S270A Variant in Complex with the Aldouronic Acid UM4X within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na509

b:17.2
occ:1.00
HO2 B:GOL507 2.2 21.3 1.0
O B:ILE259 2.4 15.2 1.0
O3 B:GOL507 2.4 19.7 1.0
O B:HOH806 2.4 20.6 1.0
O B:HOH804 2.4 18.2 1.0
O B:HOH812 2.5 19.3 1.0
O2 B:GOL507 2.5 17.8 1.0
HO3 B:GOL507 2.9 23.6 1.0
C3 B:GOL507 3.2 18.1 1.0
C2 B:GOL507 3.3 21.0 1.0
H12 B:GOL507 3.5 26.8 1.0
C B:ILE259 3.5 15.4 1.0
H31 B:GOL507 3.5 21.8 1.0
N B:ILE259 3.9 15.9 1.0
O B:HOH800 3.9 19.5 1.0
C1 B:GOL507 3.9 22.3 1.0
H32 B:GOL507 4.1 21.8 1.0
H2 B:GOL507 4.1 25.2 1.0
CA B:ILE259 4.2 13.6 1.0
HO1 B:GOL507 4.3 26.3 1.0
CA B:PRO255 4.4 19.0 1.0
O B:HOH751 4.4 22.5 1.0
O B:ASN181 4.4 17.0 1.0
N B:ASN260 4.5 15.4 1.0
O B:HOH904 4.6 33.6 1.0
O1 B:GOL507 4.6 21.9 1.0
O B:LEU251 4.6 15.2 1.0
CG2 B:THR261 4.6 15.5 1.0
O B:PRO255 4.6 18.9 1.0
O B:HOH912 4.7 22.1 1.0
H11 B:GOL507 4.7 26.8 1.0
N B:THR261 4.7 14.0 1.0
CB B:ILE259 4.8 14.1 1.0
OG1 B:THR261 4.8 15.6 1.0
CA B:ASN260 4.8 15.0 1.0
O B:THR254 4.8 17.8 1.0
C B:GLN258 4.9 16.2 1.0
C B:PRO255 5.0 19.4 1.0

Reference:

H.A.Ernst, C.Mosbech, A.E.Langkilde, P.Westh, A.S.Meyer, J.W.Agger, S.Larsen. The Structural Basis of Fungal Glucuronoyl Esterase Activity on Natural Substrates. Nat Commun V. 11 1026 2020.
ISSN: ESSN 2041-1723
PubMed: 32094331
DOI: 10.1038/S41467-020-14833-9
Page generated: Tue Oct 8 13:19:53 2024

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