Mercury in PDB 2x1x: Crystal Structure of Vegf-C in Complex with Domains 2 and 3 of VEGFR2 in A Tetragonal Crystal Form

The structure of Crystal Structure of Vegf-C in Complex with Domains 2 and 3 of VEGFR2 in A Tetragonal Crystal Form, PDB code: 2x1x was solved by V.-M.Leppanen, A.E.Prota, M.Jeltsch, A.Anisimov, N.Kalkkinen, T.Strandin, H.Lankinen, A.Goldman, K.Ballmer-Hofer, K.Alitalo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.00 / 3.10
Space group	P 42 21 2
Cell size a, b, c (Å), α, β, γ (°)	88.733, 88.733, 105.273, 90.00, 90.00, 90.00
R / Rfree (%)	26.6 / 33.4

The binding sites of Mercury atom in the Crystal Structure of Vegf-C in Complex with Domains 2 and 3 of VEGFR2 in A Tetragonal Crystal Form (pdb code 2x1x). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total only one binding site of Mercury was determined in the Crystal Structure of Vegf-C in Complex with Domains 2 and 3 of VEGFR2 in A Tetragonal Crystal Form, PDB code: 2x1x:

Mercury binding site 1 out of 1 in the Crystal Structure of Vegf-C in Complex with Domains 2 and 3 of VEGFR2 in A Tetragonal Crystal Form


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Crystal Structure of Vegf-C in Complex with Domains 2 and 3 of VEGFR2 in A Tetragonal Crystal Form within 5.0Å range: probe atom residue distance (Å) B Occ R:Hg401 b:0.2 occ:1.00 O R:HOH505 2.3 13.7 1.0 SG R:CYS162 2.4 52.3 1.0 CB R:CYS162 3.2 49.4 1.0 NH2 R:ARG169 3.3 48.0 1.0 CZ R:ARG169 3.7 47.8 1.0 CA R:CYS162 4.2 49.0 1.0 NE R:ARG169 4.2 45.6 1.0 NH1 R:ARG169 4.2 47.7 1.0 OE2 R:GLU201 4.3 53.3 1.0 OE1 R:GLU201 4.5 53.2 1.0 CD R:GLU201 4.7 53.1 1.0 CZ R:PHE199 4.7 49.9 1.0 CG R:ARG169 4.9 44.1 1.0 CB R:ARG169 4.9 42.8 1.0 O R:LYS168 4.9 40.0 1.0

V.-M.Leppanen, A.E.Prota, M.Jeltsch, A.Anisimov, N.Kalkkinen, T.Strandin, H.Lankinen, A.Goldman, K.Ballmer-Hofer, K.Alitalo. Structural Determinants of Growth Factor Binding and Specificity By Vegf Receptor 2. Proc.Natl.Acad.Sci.Usa V. 107 2425 2010.
ISSN: ISSN 0027-8424
PubMed: 20145116
DOI: 10.1073/PNAS.0914318107