Calcium in PDB 4du6: Crystal Structure of Gtp Cyclohydrolase I From Yersinia Pestis Complexed with Gtp

All present enzymatic activity of Crystal Structure of Gtp Cyclohydrolase I From Yersinia Pestis Complexed with Gtp:
3.5.4.16;

The structure of Crystal Structure of Gtp Cyclohydrolase I From Yersinia Pestis Complexed with Gtp, PDB code: 4du6 was solved by N.Maltseva, Y.Kim, K.Kwon, W.F.Anderson, A.Joachimiak, Center Forstructural Genomics Of Infectious Diseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.20 / 2.11
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	174.047, 104.912, 70.070, 90.00, 96.89, 90.00
R / Rfree (%)	18 / 22.5

The binding sites of Calcium atom in the Crystal Structure of Gtp Cyclohydrolase I From Yersinia Pestis Complexed with Gtp (pdb code 4du6). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the Crystal Structure of Gtp Cyclohydrolase I From Yersinia Pestis Complexed with Gtp, PDB code: 4du6:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in the Crystal Structure of Gtp Cyclohydrolase I From Yersinia Pestis Complexed with Gtp


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Gtp Cyclohydrolase I From Yersinia Pestis Complexed with Gtp within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca305 b:0.5 occ:1.00 ND1 B:HIS112 2.8 44.5 1.0 C8 A:GTP301 3.1 64.4 0.7 SG B:CYS109 3.2 37.0 0.2 C2' A:GTP301 3.2 64.1 0.7 CB B:HIS111 3.2 49.2 1.0 SG B:CYS180 3.2 43.7 0.7 O4' A:GTP301 3.3 64.5 0.0 SG B:CYS180 3.4 62.4 0.3 C1' A:GTP301 3.5 63.9 0.1 CE1 B:HIS112 3.5 44.9 1.0 CB B:CYS180 3.5 42.0 0.3 N9 A:GTP301 3.6 63.0 1.0 C5' A:GTP301 3.6 65.0 0.8 CB B:CYS180 3.6 41.2 0.7 C3' A:GTP301 3.7 64.4 0.6 C4' A:GTP301 3.7 65.0 0.7 CG B:HIS112 3.8 43.4 1.0 N B:HIS112 4.0 41.9 1.0 SG B:CYS109 4.0 64.4 0.8 ND1 B:HIS111 4.1 65.3 1.0 CG B:HIS111 4.1 58.9 1.0 CB B:HIS112 4.1 38.7 1.0 CA B:HIS111 4.2 46.2 1.0 C B:HIS111 4.2 43.5 1.0 N7 A:GTP301 4.3 62.9 1.0 O2' A:GTP301 4.3 64.4 0.9 O A:HOH426 4.4 71.5 1.0 CB B:CYS109 4.6 41.0 0.2 CB B:CYS109 4.6 41.3 0.8 N B:HIS111 4.6 42.5 1.0 NE2 B:HIS112 4.7 47.9 1.0 CA B:HIS112 4.7 41.4 1.0 C4 A:GTP301 4.8 60.7 0.6 CD2 B:HIS112 4.9 44.7 1.0 O5' A:GTP301 5.0 65.4 0.2 O B:HIS111 5.0 41.3 1.0 O3G A:GTP301 5.0 59.7 0.6 CA B:CYS180 5.0 40.7 0.3

Calcium binding site 2 out of 3 in the Crystal Structure of Gtp Cyclohydrolase I From Yersinia Pestis Complexed with Gtp


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of Gtp Cyclohydrolase I From Yersinia Pestis Complexed with Gtp within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca304 b:0.9 occ:1.00 ND1 C:HIS112 2.9 45.6 1.0 C8 B:GTP304 3.0 57.3 0.8 CB C:HIS111 3.1 55.1 1.0 SG C:CYS180 3.2 34.3 0.4 SG C:CYS180 3.2 0.1 0.6 SG C:CYS109 3.3 75.3 1.0 C2' B:GTP304 3.3 57.7 0.6 CB C:CYS180 3.4 38.1 0.6 CB C:CYS180 3.5 39.3 0.4 N9 B:GTP304 3.6 56.8 0.9 N C:HIS112 3.6 46.4 1.0 C1' B:GTP304 3.7 57.7 0.2 CG C:HIS112 3.8 45.3 1.0 CB C:HIS112 3.8 44.5 1.0 CA C:HIS111 3.8 49.7 1.0 C C:HIS111 3.9 47.1 1.0 O4' B:GTP304 3.9 58.3 0.1 CE1 C:HIS112 3.9 47.2 1.0 CG C:HIS111 4.0 62.9 1.0 O2' B:GTP304 4.0 54.6 1.0 N7 B:GTP304 4.0 56.8 1.0 N C:HIS111 4.1 45.7 1.0 CB C:CYS109 4.1 45.9 1.0 ND1 C:HIS111 4.2 68.2 1.0 C3' B:GTP304 4.2 59.0 0.5 C4' B:GTP304 4.4 59.1 0.4 CA C:HIS112 4.4 46.6 1.0 C5' B:GTP304 4.4 59.2 0.8 O C:HIS111 4.6 47.0 1.0 C4 B:GTP304 4.8 55.2 0.5 CA C:CYS180 4.9 38.1 0.6 CD2 C:HIS112 5.0 45.9 1.0 CA C:CYS180 5.0 38.2 0.4

Calcium binding site 3 out of 3 in the Crystal Structure of Gtp Cyclohydrolase I From Yersinia Pestis Complexed with Gtp


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Crystal Structure of Gtp Cyclohydrolase I From Yersinia Pestis Complexed with Gtp within 5.0Å range: probe atom residue distance (Å) B Occ D:Ca304 b:0.5 occ:1.00 ND1 D:HIS112 2.8 46.6 1.0 C8 C:GTP302 3.1 72.2 0.9 SG D:CYS109 3.2 58.1 0.8 C2' C:GTP302 3.2 74.0 0.6 CB D:HIS111 3.3 64.6 1.0 SG D:CYS180 3.3 45.6 0.5 O4' C:GTP302 3.3 74.1 0.2 CB D:CYS180 3.4 42.4 0.5 CB D:CYS180 3.4 42.4 0.5 O D:HOH422 3.4 65.8 1.0 C1' C:GTP302 3.5 73.2 0.4 N9 C:GTP302 3.5 71.5 0.7 C3' C:GTP302 3.6 74.5 0.5 SG D:CYS180 3.6 97.8 0.5 CE1 D:HIS112 3.7 48.3 1.0 C5' C:GTP302 3.7 76.4 1.0 C4' C:GTP302 3.7 75.1 0.6 CG D:HIS112 3.8 47.2 1.0 CG D:HIS111 4.1 72.2 1.0 CB D:HIS112 4.1 47.0 1.0 N D:HIS112 4.1 51.5 1.0 ND1 D:HIS111 4.2 77.0 1.0 CA D:HIS111 4.2 59.2 1.0 N7 C:GTP302 4.3 70.1 1.0 C D:HIS111 4.3 56.2 1.0 O2' C:GTP302 4.4 74.0 0.7 O C:HOH436 4.5 0.7 1.0 N D:HIS111 4.6 56.0 1.0 CB D:CYS109 4.6 54.2 0.2 SG D:CYS109 4.7 39.2 0.2 CA D:HIS112 4.8 48.7 1.0 CA D:CYS180 4.8 41.5 0.5 C4 C:GTP302 4.8 68.1 0.6 NE2 D:HIS112 4.8 52.0 1.0 CA D:CYS180 4.8 41.6 0.5 CB D:CYS109 4.9 53.1 0.8 O D:HIS111 4.9 57.4 1.0 CD2 D:HIS112 4.9 49.0 1.0 O3' C:GTP302 5.0 74.5 0.8

N.Maltseva, Y.Kim, K.Kwon, W.F.Anderson, A.Joachimiak, Csgid. Crystal Structure of Gtp Cyclohydrolase I From Yersinia Pestis Complexed with Gtp To Be Published.