Tungsten in PDB 2hcm: Crystal Structure of Mouse Putative Dual Specificity Phosphatase Complexed with Zinc Tungstate, New York Structural Genomics Consortium

The structure of Crystal Structure of Mouse Putative Dual Specificity Phosphatase Complexed with Zinc Tungstate, New York Structural Genomics Consortium, PDB code: 2hcm was solved by Y.Patskovsky, S.C.Almo, S.K.Burley, New York Sgx Research Center Forstructural Genomics (Nysgxrc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.00
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	53.207, 53.207, 174.485, 90.00, 90.00, 120.00
R / Rfree (%)	15 / 19.6

The structure of Crystal Structure of Mouse Putative Dual Specificity Phosphatase Complexed with Zinc Tungstate, New York Structural Genomics Consortium also contains other interesting chemical elements:

Zinc	(Zn)	2 atoms
Sodium	(Na)	1 atom

The binding sites of Tungsten atom in the Crystal Structure of Mouse Putative Dual Specificity Phosphatase Complexed with Zinc Tungstate, New York Structural Genomics Consortium (pdb code 2hcm). This binding sites where shown within 5.0 Angstroms radius around Tungsten atom.
In total only one binding site of Tungsten was determined in the Crystal Structure of Mouse Putative Dual Specificity Phosphatase Complexed with Zinc Tungstate, New York Structural Genomics Consortium, PDB code: 2hcm:

Tungsten binding site 1 out of 1 in the Crystal Structure of Mouse Putative Dual Specificity Phosphatase Complexed with Zinc Tungstate, New York Structural Genomics Consortium


Mono view


Stereo pair view

A full contact list of Tungsten with other atoms in the W binding site number 1 of Crystal Structure of Mouse Putative Dual Specificity Phosphatase Complexed with Zinc Tungstate, New York Structural Genomics Consortium within 5.0Å range: probe atom residue distance (Å) B Occ A:W366 b:28.0 occ:0.90 W A:WO4366 0.0 28.0 0.9 O3 A:WO4366 1.8 27.1 0.9 O4 A:WO4366 1.8 31.6 0.9 O2 A:WO4366 1.8 39.1 0.9 O1 A:WO4366 1.8 68.5 0.9 ZN A:ZN367 3.1 41.5 0.9 ZN A:ZN368 3.1 45.5 0.9 O A:HOH469 3.1 41.7 1.0 NH1 A:ARG101 3.8 19.5 1.0 NE2 A:GLN47 4.0 23.7 1.0 NH2 A:ARG101 4.0 23.8 1.0 NH1 A:ARG45 4.1 37.8 0.5 O A:HOH470 4.1 44.4 1.0 N A:ARG45 4.2 23.4 1.0 N A:GLN46 4.2 30.6 1.0 CB A:SER44 4.2 21.0 1.0 O A:HOH472 4.4 37.8 1.0 CZ A:ARG101 4.4 23.2 1.0 CG A:GLN47 4.5 20.6 1.0 CB A:GLN46 4.7 34.9 1.0 CD A:GLN47 4.8 24.8 1.0 CG A:GLN46 4.8 53.3 1.0 CA A:SER44 4.8 20.5 1.0 CG A:ARG45 4.8 41.1 0.5 O A:HOH507 4.8 49.6 1.0 CB A:ARG45 4.9 29.4 0.5 N A:GLN47 4.9 25.4 1.0 CA A:ARG45 4.9 28.7 0.5 CA A:GLN46 4.9 33.0 1.0 OG A:SER44 4.9 23.2 1.0 CA A:ARG45 4.9 26.8 0.5 CZ A:ARG45 5.0 47.3 0.5 CB A:ARG45 5.0 27.2 0.5

S.C.Almo, J.B.Bonanno, J.M.Sauder, S.Emtage, T.P.Dilorenzo, V.Malashkevich, S.R.Wasserman, S.Swaminathan, S.Eswaramoorthy, R.Agarwal, D.Kumaran, M.Madegowda, S.Ragumani, Y.Patskovsky, J.Alvarado, U.A.Ramagopal, J.Faber-Barata, M.R.Chance, A.Sali, A.Fiser, Z.Y.Zhang, D.S.Lawrence, S.K.Burley. Structural Genomics of Protein Phosphatases. J.Struct.Funct.Genom. V. 8 121 2007.
ISSN: ISSN 1345-711X
PubMed: 18058037
DOI: 10.1007/S10969-007-9036-1