Sodium in PDB 5i8u: Crystal Structure of the RV1700 (Mt Adprase) E142Q Mutant

All present enzymatic activity of Crystal Structure of the RV1700 (Mt Adprase) E142Q Mutant:
3.6.1.13;

The structure of Crystal Structure of the RV1700 (Mt Adprase) E142Q Mutant, PDB code: 5i8u was solved by P.Thirawatananond, L.-W.Kang, L.M.Amzel, S.B.Gabelli, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	141.42 / 2.00
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	152.768, 124.844, 142.959, 90.00, 98.50, 90.00
R / Rfree (%)	22.2 / 25.8

The binding sites of Sodium atom in the Crystal Structure of the RV1700 (Mt Adprase) E142Q Mutant (pdb code 5i8u). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Crystal Structure of the RV1700 (Mt Adprase) E142Q Mutant, PDB code: 5i8u:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Crystal Structure of the RV1700 (Mt Adprase) E142Q Mutant


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 RV1700 (Mt Adprase) E142Q Mutant within 5.0Å range: probe atom residue distance (Å) B Occ C:Na402 b:70.8 occ:1.00 OE2 C:GLU93 2.6 50.3 1.0 O C:HOH509 2.9 0.6 1.0 O1 C:FMT401 3.2 0.6 1.0 OE1 C:GLU96 3.3 58.4 1.0 CD C:GLU93 3.5 47.4 1.0 OE1 C:GLU93 3.5 50.9 1.0 C C:FMT401 3.9 0.4 1.0 O2 C:FMT401 3.9 93.4 1.0 ND1 C:HIS140 3.9 0.9 1.0 CG C:HIS140 3.9 0.6 1.0 CD2 C:HIS140 4.0 0.9 1.0 CE1 C:HIS140 4.0 0.2 1.0 NE2 C:HIS140 4.0 0.7 1.0 CB C:GLU96 4.0 44.2 1.0 CG C:GLU97 4.1 49.0 1.0 OE2 C:GLU97 4.3 62.9 1.0 CD C:GLU96 4.3 56.9 1.0 CB C:HIS140 4.5 0.9 1.0 CD C:GLU97 4.6 54.1 1.0 CG C:GLU96 4.7 51.5 1.0 NH2 C:ARG92 5.0 55.8 1.0 CG C:GLU93 5.0 44.1 1.0

Sodium binding site 2 out of 2 in the Crystal Structure of the RV1700 (Mt Adprase) E142Q Mutant


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Crystal Structure of the RV1700 (Mt Adprase) E142Q Mutant within 5.0Å range: probe atom residue distance (Å) B Occ C:Na403 b:62.2 occ:1.00 O C:HOH525 2.9 46.7 1.0 N C:GLY44 2.9 37.3 1.0 O C:HOH550 3.1 45.7 1.0 O C:PRO197 3.3 50.2 1.0 CD1 C:PHE43 3.8 43.7 1.0 CA C:PHE43 3.8 43.4 1.0 CA C:GLY44 3.8 39.6 1.0 C C:PHE43 3.8 39.7 1.0 C C:PRO197 4.0 49.3 1.0 CB C:LEU79 4.0 47.3 1.0 CB C:PRO197 4.0 45.0 1.0 CD1 C:LEU79 4.0 48.8 1.0 CB C:PHE43 4.2 42.1 1.0 CB C:ALA201 4.4 49.3 1.0 O C:HOH586 4.5 41.2 1.0 CG C:PHE43 4.5 43.1 1.0 CA C:PRO197 4.6 45.3 1.0 CG C:LEU79 4.6 45.9 1.0 CG C:PRO197 4.6 42.4 1.0 CD C:PRO197 4.6 42.3 1.0 CE1 C:PHE43 4.7 45.5 1.0 C C:GLY44 4.7 39.9 1.0 O C:GLY44 4.7 36.2 1.0 O C:HIS42 4.8 48.4 1.0 N C:THR198 4.8 45.8 1.0 NH2 C:ARG196 4.8 50.9 1.0 NE C:ARG196 4.9 58.5 1.0 N C:PRO197 5.0 43.9 1.0

S.F.O'handley, P.Thirawatananond, L.W.Kang, J.E.Cunningham, J.A.Leyva, L.M.Amzel, S.B.Gabelli. Kinetic and Mutational Studies of the Adenosine Diphosphate Ribose Hydrolase From Mycobacterium Tuberculosis. J. Bioenerg. Biomembr. V. 48 557 2016.
ISSN: ISSN 1573-6881
PubMed: 27683242
DOI: 10.1007/S10863-016-9681-9