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Sodium in PDB 6s96: Crystal Structure of the Catalytic Domain of UBE2S C118A.

Enzymatic activity of Crystal Structure of the Catalytic Domain of UBE2S C118A.

All present enzymatic activity of Crystal Structure of the Catalytic Domain of UBE2S C118A.:
2.3.2.23;

Protein crystallography data

The structure of Crystal Structure of the Catalytic Domain of UBE2S C118A., PDB code: 6s96 was solved by A.K.L.Liess, S.Lorenz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.91 / 2.18
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 120.927, 120.927, 45.344, 90.00, 90.00, 120.00
R / Rfree (%) 20.4 / 24.6

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of the Catalytic Domain of UBE2S C118A. (pdb code 6s96). 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 Catalytic Domain of UBE2S C118A., PDB code: 6s96:

Sodium binding site 1 out of 1 in 6s96

Go back to Sodium Binding Sites List in 6s96
Sodium binding site 1 out of 1 in the Crystal Structure of the Catalytic Domain of UBE2S C118A.


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 Catalytic Domain of UBE2S C118A. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na201

b:20.9
occ:1.00
OD1 A:ASN124 2.4 41.5 1.0
OD1 B:ASN124 2.5 36.5 1.0
O A:PRO123 2.8 39.5 1.0
O B:PRO123 2.9 36.3 1.0
O A:HIS122 2.9 35.7 1.0
O B:HIS122 2.9 30.1 1.0
C B:PRO123 3.5 35.1 1.0
C B:HIS122 3.5 31.3 1.0
C A:HIS122 3.6 35.6 1.0
C A:PRO123 3.6 39.5 1.0
CG A:ASN124 3.6 42.2 1.0
CB B:HIS122 3.7 34.8 1.0
CG B:ASN124 3.7 37.8 1.0
CB A:HIS122 3.7 36.9 1.0
O B:HOH303 3.8 43.5 1.0
O B:HOH309 3.9 41.7 1.0
N B:ASN124 4.0 37.1 1.0
CA B:ASN124 4.1 38.5 1.0
CA A:ASN124 4.1 43.4 1.0
CA B:HIS122 4.2 31.1 1.0
N A:ASN124 4.2 40.8 1.0
CA A:HIS122 4.2 35.5 1.0
N B:PRO123 4.3 32.1 1.0
N A:PRO123 4.3 36.6 1.0
CB B:ASN124 4.4 38.8 1.0
CA B:PRO123 4.5 32.3 1.0
CB A:ASN124 4.5 41.9 1.0
ND2 A:ASN124 4.5 39.6 1.0
CA A:PRO123 4.5 35.7 1.0
ND2 B:ASN124 4.7 36.9 1.0
CG B:HIS122 4.9 33.5 1.0

Reference:

A.K.L.Liess, A.Kucerova, K.Schweimer, D.Schlesinger, O.Dybkov, H.Urlaub, J.Mansfeld, S.Lorenz. Dimerization Regulates the Human Apc/C-Associated Ubiquitin-Conjugating Enzyme UBE2S. Sci.Signal. V. 13 2020.
ISSN: ESSN 1937-9145
PubMed: 33082289
DOI: 10.1126/SCISIGNAL.ABA8208
Page generated: Tue Dec 15 12:58:09 2020

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