Vanadium in PDB 4ri4: Crystal Structure of PTPN3 (PTPH1) Y676I Mutant in Complex with Vanadate

All present enzymatic activity of Crystal Structure of PTPN3 (PTPH1) Y676I Mutant in Complex with Vanadate:
3.1.3.48;

The structure of Crystal Structure of PTPN3 (PTPH1) Y676I Mutant in Complex with Vanadate, PDB code: 4ri4 was solved by K.-E.Chen, T.C.Meng, A.H.-J.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.00 / 1.60
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	94.878, 99.406, 134.267, 90.00, 90.00, 90.00
R / Rfree (%)	16.3 / 18.9

The binding sites of Vanadium atom in the Crystal Structure of PTPN3 (PTPH1) Y676I Mutant in Complex with Vanadate (pdb code 4ri4). This binding sites where shown within 5.0 Angstroms radius around Vanadium atom.
In total 2 binding sites of Vanadium where determined in the Crystal Structure of PTPN3 (PTPH1) Y676I Mutant in Complex with Vanadate, PDB code: 4ri4:
Jump to Vanadium binding site number: 1; 2;

Vanadium binding site 1 out of 2 in the Crystal Structure of PTPN3 (PTPH1) Y676I Mutant in Complex with 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 PTPN3 (PTPH1) Y676I Mutant in Complex with Vanadate within 5.0Å range: probe atom residue distance (Å) B Occ A:V1001 b:12.6 occ:0.80 V A:VO41001 0.0 12.6 0.8 O2 A:VO41001 1.8 17.1 1.0 O3 A:VO41001 1.8 19.1 1.0 O4 A:VO41001 1.8 18.5 1.0 O1 A:VO41001 2.0 17.5 1.0 SG A:CYS842 2.5 58.5 1.0 H A:GLY847 2.9 17.6 1.0 H A:ALA844 3.0 18.0 1.0 HE A:ARG848 3.1 18.3 1.0 HH21 A:ARG848 3.1 19.5 1.0 H A:ARG848 3.2 16.7 1.0 HB2 A:CYS842 3.2 18.9 1.0 H A:SER843 3.3 17.1 1.0 H A:GLY845 3.5 19.8 1.0 H A:ILE846 3.5 16.1 1.0 HB2 A:ALA844 3.5 23.2 1.0 CB A:CYS842 3.5 15.7 1.0 HE22 A:GLN886 3.5 18.5 1.0 N A:GLY847 3.7 14.7 1.0 OD1 A:ASP811 3.7 16.5 1.0 O A:HOH1101 3.8 17.4 1.0 N A:ALA844 3.8 15.0 1.0 NE A:ARG848 3.9 15.3 1.0 HA3 A:GLY847 3.9 16.0 1.0 NH2 A:ARG848 3.9 16.3 1.0 NE2 A:GLN886 4.0 15.4 1.0 N A:SER843 4.0 14.3 1.0 N A:ARG848 4.0 13.9 1.0 HE21 A:GLN886 4.0 18.5 1.0 HB3 A:CYS842 4.0 18.9 1.0 HB2 A:ARG848 4.1 15.7 1.0 N A:GLY845 4.1 16.5 1.0 HB3 A:SER843 4.2 18.5 1.0 O A:HOH1150 4.2 25.2 1.0 CA A:GLY847 4.2 13.3 1.0 N A:ILE846 4.3 13.4 1.0 HG13 A:ILE846 4.3 21.9 1.0 CB A:ALA844 4.3 19.3 1.0 HG3 A:ARG848 4.4 17.8 1.0 CZ A:ARG848 4.4 15.7 1.0 H A:THR849 4.4 15.9 1.0 CA A:ALA844 4.5 16.3 1.0 HH22 A:ARG848 4.6 19.5 1.0 HB1 A:ALA844 4.6 23.2 1.0 CA A:CYS842 4.6 14.9 1.0 C A:GLY847 4.7 13.6 1.0 CG A:ASP811 4.7 18.5 1.0 C A:ALA844 4.7 17.8 1.0 C A:ILE846 4.7 15.9 1.0 CA A:SER843 4.7 13.8 1.0 C A:CYS842 4.8 14.9 1.0 CB A:ARG848 4.8 13.1 1.0 C A:SER843 4.8 15.4 1.0 HG12 A:ILE846 4.8 21.9 1.0 CB A:SER843 4.9 15.4 1.0 CG A:ARG848 4.9 14.8 1.0 H A:CYS842 4.9 17.9 1.0 H A:HIS812 4.9 19.8 1.0 CD A:GLN886 4.9 16.7 1.0 CA A:GLY845 5.0 14.3 1.0 CA A:ARG848 5.0 14.8 1.0 CG1 A:ILE846 5.0 18.2 1.0 CD A:ARG848 5.0 15.0 1.0

Vanadium binding site 2 out of 2 in the Crystal Structure of PTPN3 (PTPH1) Y676I Mutant in Complex with Vanadate


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 2 of Crystal Structure of PTPN3 (PTPH1) Y676I Mutant in Complex with Vanadate within 5.0Å range: probe atom residue distance (Å) B Occ B:V1001 b:15.6 occ:0.80 V B:VO41001 0.0 15.6 0.8 O1 B:VO41001 1.8 17.7 1.0 O2 B:VO41001 1.8 18.8 1.0 O3 B:VO41001 1.9 19.1 1.0 O4 B:VO41001 2.0 19.5 1.0 SG B:CYS842 2.5 15.8 1.0 H B:GLY847 2.9 17.0 1.0 HE B:ARG848 3.1 17.2 1.0 H B:ALA844 3.1 22.5 1.0 HH21 B:ARG848 3.2 18.8 1.0 HB2 B:CYS842 3.2 19.0 1.0 H B:ARG848 3.3 17.5 1.0 H B:SER843 3.3 18.5 1.0 HE21 B:GLN886 3.4 34.0 1.0 H B:GLY845 3.4 21.8 1.0 H B:ILE846 3.5 19.3 1.0 CB B:CYS842 3.5 15.9 1.0 HB2 B:ALA844 3.6 23.6 1.0 HE22 B:GLN886 3.6 34.0 1.0 N B:GLY847 3.7 14.2 1.0 OD1 B:ASP811 3.7 18.9 1.0 NE2 B:GLN886 3.8 28.4 1.0 O B:HOH1114 3.8 22.4 1.0 HA3 B:GLY847 3.8 16.5 1.0 N B:ALA844 3.9 18.7 1.0 NE B:ARG848 3.9 14.3 1.0 NH2 B:ARG848 4.0 15.7 1.0 N B:SER843 4.0 15.4 1.0 N B:ARG848 4.0 14.6 1.0 HB3 B:CYS842 4.1 19.0 1.0 N B:GLY845 4.1 18.1 1.0 HB3 B:SER843 4.1 23.4 1.0 HB2 B:ARG848 4.1 16.9 1.0 O B:HOH1153 4.2 28.6 1.0 CA B:GLY847 4.2 13.7 1.0 HG3 B:ARG848 4.2 18.0 1.0 N B:ILE846 4.3 16.1 1.0 CB B:ALA844 4.4 19.7 1.0 HG13 B:ILE846 4.4 24.3 1.0 CZ B:ARG848 4.4 15.7 1.0 H B:THR849 4.5 17.2 1.0 CA B:ALA844 4.5 17.3 1.0 HH22 B:ARG848 4.6 18.8 1.0 C B:GLY847 4.7 16.5 1.0 CG B:ASP811 4.7 17.7 1.0 HG12 B:ILE846 4.7 24.3 1.0 CA B:CYS842 4.7 14.8 1.0 HB1 B:ALA844 4.7 23.6 1.0 C B:ALA844 4.7 20.7 1.0 CA B:SER843 4.8 16.8 1.0 C B:SER843 4.8 16.8 1.0 C B:ILE846 4.8 16.3 1.0 CB B:ARG848 4.8 14.1 1.0 H B:HIS812 4.8 22.5 1.0 C B:CYS842 4.8 16.3 1.0 CG B:ARG848 4.8 15.0 1.0 CB B:SER843 4.8 19.5 1.0 CD B:GLN886 4.9 30.8 1.0 CA B:GLY845 4.9 16.6 1.0 HA2 B:GLY845 4.9 20.0 1.0 HG1 B:THR849 5.0 22.4 1.0 CD B:ARG848 5.0 16.6 1.0 HA B:ASP811 5.0 20.4 1.0

K.E.Chen, M.Y.Li, C.C.Chou, M.R.Ho, G.C.Chen, T.C.Meng, A.H.Wang. Substrate Specificity and Plasticity of Ferm-Containing Protein Tyrosine Phosphatases. Structure 2015.
ISSN: ISSN 0969-2126
PubMed: 25728925
DOI: 10.1016/J.STR.2015.01.017