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Sodium in PDB 2yyk: Crystal Structure of the Mutant of Hpab (T198I, A276G, and R466H)

Enzymatic activity of Crystal Structure of the Mutant of Hpab (T198I, A276G, and R466H)

All present enzymatic activity of Crystal Structure of the Mutant of Hpab (T198I, A276G, and R466H):
1.14.13.3;

Protein crystallography data

The structure of Crystal Structure of the Mutant of Hpab (T198I, A276G, and R466H), PDB code: 2yyk was solved by S.-H.Kim, T.Hisano, K.Takeda, W.Iwasaki, A.Ebihara, K.Miki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.53 / 1.60
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 91.819, 99.612, 131.091, 90.00, 90.00, 90.00
R / Rfree (%) 19.5 / 20.3

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of the Mutant of Hpab (T198I, A276G, and R466H) (pdb code 2yyk). 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 the Mutant of Hpab (T198I, A276G, and R466H), PDB code: 2yyk:

Sodium binding site 1 out of 1 in 2yyk

Go back to Sodium Binding Sites List in 2yyk
Sodium binding site 1 out of 1 in the Crystal Structure of the Mutant of Hpab (T198I, A276G, and R466H)


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 the Mutant of Hpab (T198I, A276G, and R466H) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na505

b:17.6
occ:1.00
O A:HOH1750 2.0 34.8 1.0
OE2 A:GLU226 2.1 29.3 1.0
O A:HOH1747 2.3 34.2 1.0
O A:HOH1748 2.3 46.3 1.0
O A:HOH1749 2.3 36.0 1.0
CD A:GLU226 2.9 23.0 1.0
OE1 A:GLU226 3.0 23.3 1.0
O A:HOH1850 3.7 41.3 1.0
NZ A:LYS22 4.0 42.4 1.0
O A:HOH1760 4.2 27.2 1.0
O A:HOH1844 4.2 39.5 1.0
CG A:GLU226 4.3 21.8 1.0
CE A:LYS22 4.4 40.7 1.0

Reference:

S.-H.Kim, T.Hisano, K.Takeda, W.Iwasaki, A.Ebihara, K.Miki. Crystal Structure of the Oxygenase Component (Hpab) of the 4-Hydroxyphenylacetate 3-Monooxygenase From Thermus Thermophilus HB8 J.Biol.Chem. V. 282 33107 2007.
ISSN: ISSN 0021-9258
PubMed: 17804419
DOI: 10.1074/JBC.M703440200
Page generated: Tue Dec 15 06:00:50 2020

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