Vanadium in PDB 6lvq: Crystal Structure of DUSP22_VO4

All present enzymatic activity of Crystal Structure of DUSP22_VO4:
3.1.3.16; 3.1.3.48;

The structure of Crystal Structure of DUSP22_VO4, PDB code: 6lvq was solved by C.H.Lai, P.C.Lyu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.26 / 1.38
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	36.130, 49.736, 39.847, 90.00, 108.13, 90.00
R / Rfree (%)	20.4 / 22.9

The binding sites of Vanadium atom in the Crystal Structure of DUSP22_VO4 (pdb code 6lvq). 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 DUSP22_VO4, PDB code: 6lvq:

Vanadium binding site 1 out of 1 in the Crystal Structure of DUSP22_VO4


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 DUSP22_VO4 within 5.0Å range: probe atom residue distance (Å) B Occ A:V201 b:17.8 occ:1.00 V A:VO4201 0.0 17.8 1.0 O4 A:VO4201 1.8 16.0 1.0 O2 A:VO4201 1.8 14.1 1.0 O1 A:VO4201 1.8 14.1 1.0 O3 A:VO4201 1.8 20.4 1.0 SG A:CYS88 2.7 14.0 1.0 CB A:CYS88 3.6 14.5 1.0 NH2 A:ARG94 3.7 19.9 1.0 NE A:ARG94 3.8 16.1 1.0 N A:SER93 3.9 12.1 1.0 N A:ALA90 3.9 13.0 1.0 O A:HOH370 4.0 29.1 1.0 N A:ARG94 4.0 11.7 1.0 OD2 A:ASP57 4.0 22.1 1.0 CB A:SER93 4.2 16.1 1.0 CZ A:ARG94 4.2 17.5 1.0 N A:LEU89 4.2 14.0 1.0 N A:VAL92 4.3 11.9 1.0 CB A:ALA90 4.3 13.2 1.0 N A:GLY91 4.3 11.3 1.0 CG A:ASP57 4.4 21.1 1.0 CA A:SER93 4.5 14.2 1.0 CA A:ALA90 4.5 11.4 1.0 CB A:ASP57 4.6 21.4 1.0 CB A:ARG94 4.6 14.3 1.0 C A:SER93 4.8 12.4 1.0 C A:ALA90 4.8 12.0 1.0 CA A:CYS88 4.8 12.5 1.0 CG A:ARG94 4.9 13.6 1.0 CB A:LEU89 4.9 14.6 1.0 C A:CYS88 4.9 13.6 1.0 CA A:LEU89 4.9 14.8 1.0 CD A:ARG94 4.9 17.5 1.0 C A:VAL92 4.9 12.1 1.0 C A:LEU89 4.9 13.4 1.0 CA A:VAL92 5.0 14.6 1.0 CA A:ARG94 5.0 12.0 1.0

C.H.Lai, C.C.Chang, H.C.Chuang, T.H.Tan, P.C.Lyu. Structural Insights Into the Active Site Formation of DUSP22 in N-Loop-Containing Protein Tyrosine Phosphatases. Int J Mol Sci V. 21 2020.
ISSN: ESSN 1422-0067
PubMed: 33053837
DOI: 10.3390/IJMS21207515