Vanadium in PDB 6dt6: Crystal Structure of the Yoph PTP1B Chimera 3 Ptpase Bound to Vanadate

The structure of Crystal Structure of the Yoph PTP1B Chimera 3 Ptpase Bound to Vanadate, PDB code: 6dt6 was solved by Y.Morales, S.J.Johnson, A.C.Hengge, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.57 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	49.125, 54.781, 96.791, 90.00, 90.00, 90.00
R / Rfree (%)	17.5 / 22.7

The binding sites of Vanadium atom in the Crystal Structure of the Yoph PTP1B Chimera 3 Ptpase Bound to Vanadate (pdb code 6dt6). This binding sites where shown within 5.0 Angstroms radius around Vanadium atom.
In total only one binding site of Vanadium was determined in the Crystal Structure of the Yoph PTP1B Chimera 3 Ptpase Bound to Vanadate, PDB code: 6dt6:

Vanadium binding site 1 out of 1 in the Crystal Structure of the Yoph PTP1B Chimera 3 Ptpase Bound to Vanadate


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 1 of Crystal Structure of the Yoph PTP1B Chimera 3 Ptpase Bound to Vanadate within 5.0Å range: probe atom residue distance (Å) B Occ A:V501 b:59.8 occ:0.79 V A:VO4501 0.0 59.8 0.8 O2 A:VO4501 2.1 61.0 1.0 O4 A:VO4501 2.1 59.5 1.0 O3 A:VO4501 2.1 59.6 0.7 O1 A:VO4501 2.1 63.2 1.0 SG A:CYS403 3.0 39.3 1.0 CB A:CYS403 3.7 34.4 1.0 O A:HOH619 3.8 46.7 1.0 NE A:ARG409 4.1 51.6 1.0 N A:GLY408 4.1 32.2 1.0 NH2 A:ARG409 4.1 58.0 1.0 N A:ALA405 4.1 36.9 1.0 N A:ARG404 4.1 33.1 1.0 N A:ARG409 4.2 33.2 1.0 CA A:GLY408 4.2 35.7 1.0 OE1 A:GLN446 4.5 49.0 1.0 CZ A:ARG409 4.5 55.7 1.0 CB A:ARG404 4.6 42.9 1.0 CB A:ALA405 4.6 34.8 1.0 N A:GLY406 4.7 31.5 1.0 CA A:ARG404 4.8 39.5 1.0 C A:GLY408 4.8 35.3 1.0 CA A:ALA405 4.9 34.1 1.0 N A:VAL407 4.9 29.7 1.0 CG A:ARG409 4.9 35.1 1.0 CB A:ARG409 4.9 30.2 1.0 C A:ARG404 5.0 40.5 1.0 CA A:CYS403 5.0 33.0 1.0

G.Moise, Y.Morales, V.Beaumont, T.Caradonna, J.P.Loria, S.J.Johnson, A.C.Hengge. A Yoph PTP1B Chimera Shows the Importance of the Wpd-Loop Sequence to the Activity, Structure, and Dynamics of Protein Tyrosine Phosphatases. Biochemistry V. 57 5315 2018.
ISSN: ISSN 1520-4995
PubMed: 30110154
DOI: 10.1021/ACS.BIOCHEM.8B00663