Calcium in PDB 6vgc: Crystal Structures of Flap Bound to Dg-031

The structure of Crystal Structures of Flap Bound to Dg-031, PDB code: 6vgc was solved by J.D.Ho, M.R.Lee, C.T.Rauch, K.Aznavour, J.S.Park, J.G.Luz, S.Antonysamy, B.Condon, M.Maletic, A.Zhang, M.J.Hickey, N.E.Hughes, S.Chandrasekhar, A.V.Sloan, K.Gooding, A.Harvey, X.P.Yu, S.D.Kahl, B.H.Norman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.37
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	65.911, 101.488, 111.864, 90.00, 99.83, 90.00
R / Rfree (%)	25.4 / 28.5

The binding sites of Calcium atom in the Crystal Structures of Flap Bound to Dg-031 (pdb code 6vgc). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structures of Flap Bound to Dg-031, PDB code: 6vgc:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structures of Flap Bound to Dg-031


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structures of Flap Bound to Dg-031 within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca202 b:81.6 occ:1.00 OE1 B:GLN58 2.3 43.2 1.0 OE1 A:GLN58 2.4 51.1 1.0 OE1 C:GLN58 2.4 53.5 1.0 OD1 A:ASP62 3.1 41.8 1.0 OD1 B:ASP62 3.3 36.7 1.0 OD1 C:ASP62 3.4 36.8 1.0 CD B:GLN58 3.5 39.0 1.0 CD A:GLN58 3.5 45.1 1.0 CD C:GLN58 3.6 50.2 1.0 NE2 B:GLN58 4.1 32.1 1.0 NE2 A:GLN58 4.1 33.5 1.0 CG1 B:VAL61 4.1 45.8 1.0 CG A:ASP62 4.3 43.8 1.0 CG1 C:VAL61 4.3 34.9 1.0 CG C:GLN58 4.4 48.8 1.0 CG1 A:VAL61 4.5 41.5 1.0 CG B:ASP62 4.6 41.5 1.0 CG C:ASP62 4.6 34.3 1.0 CG B:GLN58 4.6 37.1 1.0 NE2 C:GLN58 4.6 47.2 1.0 CG A:GLN58 4.7 45.2 1.0 OD2 A:ASP62 5.0 46.8 1.0

Calcium binding site 2 out of 2 in the Crystal Structures of Flap Bound to Dg-031


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structures of Flap Bound to Dg-031 within 5.0Å range: probe atom residue distance (Å) B Occ D:Ca202 b:80.2 occ:1.00 OE1 F:GLN58 2.3 65.7 1.0 OE1 D:GLN58 2.4 62.9 1.0 OE1 E:GLN58 2.4 61.7 1.0 OD1 F:ASP62 2.5 56.0 1.0 CD D:GLN58 3.4 58.9 1.0 CD F:GLN58 3.5 62.0 1.0 OD1 D:ASP62 3.5 50.8 1.0 CD E:GLN58 3.6 61.9 1.0 CG F:ASP62 3.7 57.0 1.0 CG D:GLN58 3.9 59.9 1.0 CG1 D:VAL61 4.1 52.0 1.0 OD2 F:ASP62 4.1 59.0 1.0 OD1 E:ASP62 4.2 55.7 1.0 CG F:GLN58 4.2 62.3 1.0 NE2 E:GLN58 4.3 59.5 1.0 NE2 F:GLN58 4.5 55.9 1.0 NE2 D:GLN58 4.5 64.3 1.0 CG E:GLN58 4.7 58.3 1.0 CG D:ASP62 4.7 48.9 1.0 CG1 F:VAL61 4.7 57.5 1.0 CB D:VAL61 4.7 49.4 1.0 O D:GLN58 4.8 57.4 1.0 O E:HOH305 4.8 60.0 1.0 CB F:ASP62 4.9 55.1 1.0 O F:GLN58 4.9 61.8 1.0 CG1 E:VAL61 4.9 50.5 1.0 CA F:ASP62 5.0 54.9 1.0

J.D.Ho, M.R.Lee, C.T.Rauch, K.Aznavour, J.S.Park, J.G.Luz, S.Antonysamy, B.Condon, M.Maletic, A.Zhang, M.J.Hickey, N.E.Hughes, S.Chandrasekhar, A.V.Sloan, K.Gooding, A.Harvey, X.P.Yu, S.D.Kahl, B.H.Norman. Structure-Based, Multi-Targeted Drug Discovery Approach to Eicosanoid Inhibition: Dual Inhibitors of Mpges-1 and 5-Lipoxygenase Activating Protein (Flap). Biochim Biophys Acta Gen 29800 2020SUBJ.
ISSN: ISSN 1872-8006
PubMed: 33246032
DOI: 10.1016/J.BBAGEN.2020.129800