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Sodium in PDB 1g97: S.Pneumoniae Glmu Complexed with Udp-N-Acetylglucosamine and MG2+

Enzymatic activity of S.Pneumoniae Glmu Complexed with Udp-N-Acetylglucosamine and MG2+

All present enzymatic activity of S.Pneumoniae Glmu Complexed with Udp-N-Acetylglucosamine and MG2+:
2.7.7.23;

Protein crystallography data

The structure of S.Pneumoniae Glmu Complexed with Udp-N-Acetylglucosamine and MG2+, PDB code: 1g97 was solved by D.Kostrewa, A.D'arcy, M.Kamber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.96
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 93.660, 93.660, 275.900, 90.00, 90.00, 120.00
R / Rfree (%) 18.8 / 22.1

Other elements in 1g97:

The structure of S.Pneumoniae Glmu Complexed with Udp-N-Acetylglucosamine and MG2+ also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the S.Pneumoniae Glmu Complexed with Udp-N-Acetylglucosamine and MG2+ (pdb code 1g97). 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 S.Pneumoniae Glmu Complexed with Udp-N-Acetylglucosamine and MG2+, PDB code: 1g97:

Sodium binding site 1 out of 1 in 1g97

Go back to Sodium Binding Sites List in 1g97
Sodium binding site 1 out of 1 in the S.Pneumoniae Glmu Complexed with Udp-N-Acetylglucosamine and MG2+


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of S.Pneumoniae Glmu Complexed with Udp-N-Acetylglucosamine and MG2+ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na461

b:12.4
occ:0.33
O A:HOH504 2.1 9.1 1.0
OD1 A:ASN405 2.2 10.4 1.0
CG A:ASN405 3.2 16.6 1.0
ND2 A:ASN405 3.5 14.2 1.0
O A:GLY380 4.3 12.5 1.0
O A:HOH521 4.5 13.2 1.0
CB A:ASN405 4.5 12.3 1.0
CA A:ASN405 4.8 12.3 1.0

Reference:

D.Kostrewa, A.D'arcy, B.Takacs, M.Kamber. Crystal Structures of Streptococcus Pneumoniae N-Acetylglucosamine-1-Phosphate Uridyltransferase, Glmu, in Apo Form at 2.33 A Resolution and in Complex with Udp-N-Acetylglucosamine and Mg(2+) at 1.96 A Resolution. J.Mol.Biol. V. 305 279 2001.
ISSN: ISSN 0022-2836
PubMed: 11124906
DOI: 10.1006/JMBI.2000.4296
Page generated: Tue Dec 15 05:24:08 2020

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