Sodium in PDB 5tvo: Crystal Structure of Trypanosoma Brucei Adometdc-DELTA26 Monomer

All present enzymatic activity of Crystal Structure of Trypanosoma Brucei Adometdc-DELTA26 Monomer:
4.1.1.50;

The structure of Crystal Structure of Trypanosoma Brucei Adometdc-DELTA26 Monomer, PDB code: 5tvo was solved by O.A.Volkov, C.Ariagno, Z.Chen, D.R.Tomchick, M.A.Phillips, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.01 / 1.48
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	46.669, 75.644, 87.915, 90.00, 90.00, 90.00
R / Rfree (%)	15.7 / 20

The binding sites of Sodium atom in the Crystal Structure of Trypanosoma Brucei Adometdc-DELTA26 Monomer (pdb code 5tvo). 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 Trypanosoma Brucei Adometdc-DELTA26 Monomer, PDB code: 5tvo:

Sodium binding site 1 out of 1 in the Crystal Structure of Trypanosoma Brucei Adometdc-DELTA26 Monomer


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 Trypanosoma Brucei Adometdc-DELTA26 Monomer within 5.0Å range: probe atom residue distance (Å) B Occ A:Na402 b:29.2 occ:1.00 O A:HOH695 2.7 31.8 1.0 O A:HOH674 2.8 23.9 1.0 O A:HOH649 2.9 24.7 1.0 HH A:TYR352 2.9 27.4 1.0 HB1 A:ALA333 3.0 31.6 1.0 OH A:TYR352 3.0 22.8 1.0 HB A:VAL350 3.2 23.2 1.0 HG12 A:VAL350 3.2 26.9 1.0 HG11 A:VAL350 3.3 26.9 1.0 HB2 A:ALA333 3.4 31.6 1.0 HD3 A:PRO325 3.4 31.1 1.0 HG3 A:PRO325 3.5 32.2 1.0 CB A:ALA333 3.6 26.3 1.0 CG1 A:VAL350 3.6 22.4 1.0 CZ A:TYR352 3.6 21.5 1.0 HB2 A:ARG336 3.8 32.0 1.0 O A:VAL323 3.9 21.1 1.0 HA A:GLU324 3.9 26.1 1.0 CB A:VAL350 3.9 19.4 1.0 HE2 A:TYR352 4.0 24.5 1.0 HB3 A:ALA333 4.0 31.6 1.0 CE2 A:TYR352 4.1 20.4 1.0 HD3 A:ARG336 4.1 40.0 1.0 O A:HOH651 4.2 27.4 1.0 CD A:PRO325 4.2 25.9 1.0 CG A:PRO325 4.2 26.9 1.0 CE1 A:TYR352 4.4 21.1 1.0 HE1 A:TYR352 4.5 25.3 1.0 HG13 A:VAL350 4.5 26.9 1.0 HG21 A:VAL350 4.6 24.5 1.0 HA A:VAL350 4.6 21.1 1.0 HG2 A:PRO325 4.6 32.2 1.0 H A:ASN351 4.7 24.3 1.0 CB A:ARG336 4.8 26.7 1.0 CA A:GLU324 4.8 21.7 1.0 HG23 A:VAL323 4.8 27.1 1.0 N A:PRO325 4.8 23.8 1.0 HA A:ALA333 4.8 28.7 1.0 CA A:ALA333 4.9 23.9 1.0 O A:HOH699 4.9 41.2 1.0 CG2 A:VAL350 4.9 20.4 1.0 C A:VAL323 4.9 19.3 1.0 CA A:VAL350 4.9 17.6 1.0 HG3 A:ARG336 4.9 35.8 1.0 HD2 A:PRO325 5.0 31.1 1.0 O A:HOH670 5.0 44.3 1.0 CD A:ARG336 5.0 33.4 1.0

O.A.Volkov, L.N.Kinch, C.Ariagno, X.Deng, S.Zhong, N.V.Grishin, D.R.Tomchick, Z.Chen, M.A.Phillips. Relief of Autoinhibition By Conformational Switch Explains Enzyme Activation By A Catalytically Dead Paralog. Elife V. 5 2016.
ISSN: ESSN 2050-084X
PubMed: 27977001
DOI: 10.7554/ELIFE.20198