Tungsten in PDB 6ohm: Structure of Tungstate Bound Human Phospholipase D2 Catalytic Domain

All present enzymatic activity of Structure of Tungstate Bound Human Phospholipase D2 Catalytic Domain:
3.1.4.4;

The structure of Structure of Tungstate Bound Human Phospholipase D2 Catalytic Domain, PDB code: 6ohm was solved by C.M.Metrick, J.V.Chodaparambil, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.55 / 1.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	92.515, 132.242, 107.089, 90.00, 111.45, 90.00
R / Rfree (%)	18.2 / 20.6

The binding sites of Tungsten atom in the Structure of Tungstate Bound Human Phospholipase D2 Catalytic Domain (pdb code 6ohm). This binding sites where shown within 5.0 Angstroms radius around Tungsten atom.
In total 2 binding sites of Tungsten where determined in the Structure of Tungstate Bound Human Phospholipase D2 Catalytic Domain, PDB code: 6ohm:
Jump to Tungsten binding site number: 1; 2;

Tungsten binding site 1 out of 2 in the Structure of Tungstate Bound Human Phospholipase D2 Catalytic Domain


Mono view


Stereo pair view

A full contact list of Tungsten with other atoms in the W binding site number 1 of Structure of Tungstate Bound Human Phospholipase D2 Catalytic Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:W1001 b:35.3 occ:1.00 W A:WO41001 0.0 35.3 1.0 O2 A:WO41001 2.0 34.4 1.0 O4 A:WO41001 2.0 32.7 1.0 O3 A:WO41001 2.0 38.0 1.0 O1 A:WO41001 2.0 33.7 1.0 NE2 A:HIS442 2.5 15.9 1.0 O A:HOH1105 2.6 33.7 1.0 NE2 A:HIS756 3.4 17.5 1.0 CD2 A:HIS442 3.4 16.8 1.0 CE1 A:HIS442 3.5 16.5 1.0 OE1 A:GLN642 3.8 20.4 1.0 CE1 A:HIS756 3.9 17.8 1.0 O A:HOH1139 4.1 16.6 1.0 NZ A:LYS444 4.1 11.3 1.0 NZ A:LYS758 4.4 12.3 1.0 ND2 A:ASN773 4.5 15.7 1.0 CD2 A:HIS756 4.5 17.5 1.0 ND1 A:HIS442 4.6 16.4 1.0 CG A:HIS442 4.6 16.0 1.0 CE A:LYS444 4.6 11.6 1.0 CD A:GLN642 4.7 20.2 1.0 NE2 A:GLN642 4.7 21.0 1.0 CE A:LYS758 4.8 12.3 1.0

Tungsten binding site 2 out of 2 in the Structure of Tungstate Bound Human Phospholipase D2 Catalytic Domain


Mono view


Stereo pair view

A full contact list of Tungsten with other atoms in the W binding site number 2 of Structure of Tungstate Bound Human Phospholipase D2 Catalytic Domain within 5.0Å range: probe atom residue distance (Å) B Occ B:W1001 b:36.1 occ:1.00 W B:WO41001 0.0 36.1 1.0 O2 B:WO41001 2.0 35.9 1.0 O3 B:WO41001 2.0 35.8 1.0 O1 B:WO41001 2.0 36.1 1.0 O4 B:WO41001 2.1 37.8 1.0 NE2 B:HIS442 2.5 17.5 1.0 NE2 B:HIS756 3.3 18.1 1.0 CD2 B:HIS442 3.4 19.4 1.0 CE1 B:HIS442 3.5 17.8 1.0 CE1 B:HIS756 3.8 18.5 1.0 OE1 B:GLN642 3.8 21.3 1.0 O B:HOH1134 3.9 21.1 1.0 NZ B:LYS444 4.2 12.7 1.0 CD2 B:HIS756 4.4 18.0 1.0 NZ B:LYS758 4.5 11.6 1.0 ND2 B:ASN773 4.5 14.8 1.0 ND1 B:HIS442 4.6 18.5 1.0 CG B:HIS442 4.6 18.5 1.0 CE B:LYS444 4.7 13.6 1.0 CD B:GLN642 4.7 19.0 1.0 NE2 B:GLN642 4.7 18.9 1.0 O B:HOH1427 4.7 46.2 1.0 CE B:LYS758 4.8 11.6 1.0 O B:HOH1394 4.9 49.1 1.0

C.M.Metrick, E.A.Peterson, J.C.Santoro, I.J.Enyedy, P.Murugan, T.Chen, K.Michelsen, M.Cullivan, K.A.Spilker, P.R.Kumar, T.L.May-Dracka, J.V.Chodaparambil. Human Pld Structures Enable Drug Design and Characterization of Isoenzyme Selectivity. Nat.Chem.Biol. 2020.
ISSN: ESSN 1552-4469
PubMed: 32042197
DOI: 10.1038/S41589-019-0458-4