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Sodium in PDB 4m99: Acetyltransferase Domain of Pglb From Neisseria Gonorrhoeae FA1090 in Complex with Acetyl Coenzyme A

Protein crystallography data

The structure of Acetyltransferase Domain of Pglb From Neisseria Gonorrhoeae FA1090 in Complex with Acetyl Coenzyme A, PDB code: 4m99 was solved by M.J.Morrison, B.Imperiali, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 64.18 / 2.60
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 97.660, 97.660, 173.910, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / 22.7

Sodium Binding Sites:

The binding sites of Sodium atom in the Acetyltransferase Domain of Pglb From Neisseria Gonorrhoeae FA1090 in Complex with Acetyl Coenzyme A (pdb code 4m99). 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 Acetyltransferase Domain of Pglb From Neisseria Gonorrhoeae FA1090 in Complex with Acetyl Coenzyme A, PDB code: 4m99:

Sodium binding site 1 out of 1 in 4m99

Go back to Sodium Binding Sites List in 4m99
Sodium binding site 1 out of 1 in the Acetyltransferase Domain of Pglb From Neisseria Gonorrhoeae FA1090 in Complex with Acetyl Coenzyme A


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Acetyltransferase Domain of Pglb From Neisseria Gonorrhoeae FA1090 in Complex with Acetyl Coenzyme A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na502

b:59.2
occ:1.00
NE2 A:HIS348 2.6 45.0 1.0
NE2 B:HIS348 2.6 48.3 1.0
NE2 C:HIS348 2.7 49.3 1.0
CE1 B:HIS348 3.1 49.0 1.0
CE1 A:HIS348 3.2 49.7 1.0
CE1 C:HIS348 3.3 44.9 1.0
CD2 A:HIS348 3.8 46.7 1.0
CD2 B:HIS348 3.9 46.4 1.0
CD2 C:HIS348 3.9 47.4 1.0
O B:GLY346 4.2 48.5 1.0
O A:GLY346 4.3 48.9 1.0
O C:GLY346 4.4 44.7 1.0
ND1 B:HIS348 4.4 46.6 1.0
ND1 A:HIS348 4.4 47.0 1.0
CA B:GLY346 4.4 45.5 1.0
O B:ALA328 4.6 44.1 1.0
ND1 C:HIS348 4.6 39.3 1.0
CA A:GLY346 4.6 42.5 1.0
CA C:GLY346 4.7 43.7 1.0
CG A:HIS348 4.8 48.7 1.0
C B:GLY346 4.8 47.7 1.0
O A:ALA328 4.8 43.0 1.0
O C:ALA328 4.8 41.7 1.0
CG B:HIS348 4.8 48.3 1.0
C A:GLY346 4.9 44.7 1.0
CG C:HIS348 4.9 49.5 1.0
C C:GLY346 5.0 45.6 1.0

Reference:

M.J.Morrison, B.Imperiali. Biochemical Analysis and Structure Determination of Bacterial Acetyltransferases Responsible For the Biosynthesis of Udp-N,N'-Diacetylbacillosamine. J.Biol.Chem. V. 288 32248 2013.
ISSN: ISSN 0021-9258
PubMed: 24064219
DOI: 10.1074/JBC.M113.510560
Page generated: Mon Oct 7 16:56:21 2024

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