Zinc in PDB 3dss: Crystal Structure of Rabggtase(Delta Lrr; Delta Ig)

All present enzymatic activity of Crystal Structure of Rabggtase(Delta Lrr; Delta Ig):
2.5.1.60;

The structure of Crystal Structure of Rabggtase(Delta Lrr; Delta Ig), PDB code: 3dss was solved by Z.Guo, S.Yu, R.S.Goody, K.Alexandrov, W.Blankenfeldt, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.13 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	66.748, 90.628, 114.068, 90.00, 90.00, 90.00
R / Rfree (%)	14.9 / 19.4

The structure of Crystal Structure of Rabggtase(Delta Lrr; Delta Ig) also contains other interesting chemical elements:

Calcium

(Ca)

2 atoms

The binding sites of Zinc atom in the Crystal Structure of Rabggtase(Delta Lrr; Delta Ig) (pdb code 3dss). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Rabggtase(Delta Lrr; Delta Ig), PDB code: 3dss:

Zinc binding site 1 out of 1 in the Crystal Structure of Rabggtase(Delta Lrr; Delta Ig)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Rabggtase(Delta Lrr; Delta Ig) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn332 b:0.2 occ:1.00 NE2 B:HIS290 2.7 13.6 1.0 CB B:CYS240 3.0 12.7 1.0 OD2 B:ASP238 3.4 19.3 1.0 O B:HOH588 3.4 36.9 1.0 CE1 B:HIS290 3.5 14.6 1.0 OD1 B:ASP238 3.7 17.6 1.0 CD2 B:HIS290 3.7 13.6 1.0 CG B:ASP238 3.8 14.8 1.0 SG B:CYS240 3.9 15.6 1.0 O B:HOH451 4.0 32.1 1.0 CB B:ASP280 4.3 15.2 1.0 CA B:CYS240 4.4 12.3 1.0 CE1 B:PHE289 4.4 18.4 1.0 N B:CYS240 4.5 11.9 1.0 O B:HOH648 4.5 51.3 1.0 ND1 B:HIS290 4.7 13.6 1.0 O A:HOH589 4.8 47.6 1.0 CG B:HIS290 4.8 13.1 1.0 CB B:ASP238 4.8 12.4 1.0 CD1 B:PHE289 5.0 17.4 1.0

Z.Guo, Y.-W.Wu, D.Das, C.Delon, J.Cramer, S.Yu, S.Thuns, N.Lupilova, H.Waldmann, L.Brunsveld, R.S.Goody, K.Alexandrov, W.Blankenfeldt. Structures of Rabggtase-Substrate/Product Complexes Provide Insights Into the Evolution of Protein Prenylation Embo J. V. 27 2444 2008.
ISSN: ISSN 0261-4189
PubMed: 18756270
DOI: 10.1038/EMBOJ.2008.164