Zinc in PDB 1fbx: Crystal Structure of Zinc-Containing E.Coli Gtp Cyclohydrolase I

All present enzymatic activity of Crystal Structure of Zinc-Containing E.Coli Gtp Cyclohydrolase I:
3.5.4.16;

The structure of Crystal Structure of Zinc-Containing E.Coli Gtp Cyclohydrolase I, PDB code: 1fbx was solved by G.Auerbach, A.Herrmann, A.Bracher, A.Bader, M.Gutlich, M.Fischer, M.Neukamm, H.Nar, M.Garrido-Franco, J.Richardson, R.Huber, A.Bacher, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	14.98 / 2.80
Space group	C 2 2 21 1
Cell size a, b, c (Å), α, β, γ (°)	227.690, 314.190, 132.570, 90.00, 90.00, 90.00
R / Rfree (%)	20.2 / 25.1

The structure of Crystal Structure of Zinc-Containing E.Coli Gtp Cyclohydrolase I also contains other interesting chemical elements:

Chlorine

(Cl)

15 atoms

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 15;

Binding sites:

The binding sites of Zinc atom in the Crystal Structure of Zinc-Containing E.Coli Gtp Cyclohydrolase I (pdb code 1fbx). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 15 binding sites of Zinc where determined in the Crystal Structure of Zinc-Containing E.Coli Gtp Cyclohydrolase I, PDB code: 1fbx:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Zinc binding site 1 out of 15 in the Crystal Structure of Zinc-Containing E.Coli Gtp Cyclohydrolase I


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 Zinc-Containing E.Coli Gtp Cyclohydrolase I within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn3316 b:60.0 occ:1.00 CD2 A:HIS113 1.9 36.6 1.0 O A:HOH3331 2.1 10.6 1.0 NE2 A:HIS113 2.2 43.5 1.0 SG A:CYS110 2.2 47.7 1.0 SG A:CYS181 2.3 46.0 1.0 CB A:CYS181 3.1 34.5 1.0 CG A:HIS113 3.3 33.2 1.0 CB A:CYS110 3.3 41.3 1.0 CE1 A:HIS113 3.5 32.3 1.0 CB A:HIS112 3.6 47.5 1.0 N A:HIS113 3.9 32.7 1.0 ND1 A:HIS113 4.0 27.5 1.0 CB A:HIS113 4.3 31.2 1.0 CA A:HIS112 4.3 38.5 1.0 N A:HIS112 4.3 39.4 1.0 C A:HIS112 4.3 35.0 1.0 CG A:HIS112 4.3 59.8 1.0 ND1 A:HIS112 4.5 65.1 1.0 CA A:CYS181 4.6 33.0 1.0 CA A:HIS113 4.6 31.9 1.0 CA A:CYS110 4.7 40.1 1.0 C A:CYS110 4.9 40.1 1.0

Zinc binding site 2 out of 15 in the Crystal Structure of Zinc-Containing E.Coli Gtp Cyclohydrolase I


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Zinc-Containing E.Coli Gtp Cyclohydrolase I within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn3317 b:53.0 occ:1.00 CD2 B:HIS113 1.9 39.0 1.0 O B:HOH3332 2.2 33.3 1.0 SG B:CYS181 2.2 41.6 1.0 NE2 B:HIS113 2.2 42.8 1.0 SG B:CYS110 2.2 42.5 1.0 CB B:CYS181 2.9 30.8 1.0 CG B:HIS113 3.3 33.1 1.0 CB B:CYS110 3.3 32.8 1.0 CE1 B:HIS113 3.5 33.6 1.0 CB B:HIS112 3.9 41.8 1.0 ND1 B:HIS113 4.0 29.6 1.0 N B:HIS113 4.0 27.3 1.0 CB B:HIS113 4.2 28.2 1.0 CA B:CYS181 4.4 29.0 1.0 ND1 B:HIS112 4.4 57.4 1.0 C B:HIS112 4.5 29.7 1.0 CA B:HIS112 4.6 31.4 1.0 CG B:HIS112 4.6 52.9 1.0 N B:HIS112 4.6 31.4 1.0 CA B:HIS113 4.7 27.2 1.0 CA B:CYS110 4.8 31.7 1.0 N B:CYS181 4.9 23.6 1.0 C B:CYS181 4.9 27.1 1.0

Zinc binding site 3 out of 15 in the Crystal Structure of Zinc-Containing E.Coli Gtp Cyclohydrolase I


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Zinc-Containing E.Coli Gtp Cyclohydrolase I within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn3318 b:51.7 occ:1.00 CD2 C:HIS113 1.9 40.3 1.0 SG C:CYS181 2.2 42.5 1.0 SG C:CYS110 2.2 41.5 1.0 NE2 C:HIS113 2.2 44.5 1.0 O C:HOH3333 2.4 22.5 1.0 CB C:CYS181 2.9 29.0 1.0 CG C:HIS113 3.2 34.5 1.0 CB C:CYS110 3.3 31.9 1.0 CE1 C:HIS113 3.5 32.8 1.0 CB C:HIS112 3.7 36.5 1.0 N C:HIS113 3.9 30.0 1.0 ND1 C:HIS113 4.0 31.9 1.0 CB C:HIS113 4.1 29.3 1.0 C C:HIS112 4.3 31.7 1.0 CA C:CYS181 4.4 30.8 1.0 CA C:HIS112 4.4 33.0 1.0 N C:HIS112 4.5 32.9 1.0 CA C:HIS113 4.6 31.0 1.0 CG C:HIS112 4.7 47.1 1.0 CA C:CYS110 4.7 33.0 1.0 CD2 C:HIS112 4.8 51.6 1.0 C C:CYS181 4.9 30.0 1.0 C C:CYS110 4.9 34.7 1.0 N C:CYS181 4.9 29.4 1.0 O C:CYS181 5.0 35.3 1.0

Zinc binding site 4 out of 15 in the Crystal Structure of Zinc-Containing E.Coli Gtp Cyclohydrolase I


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Zinc-Containing E.Coli Gtp Cyclohydrolase I within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn3319 b:57.7 occ:1.00 CD2 D:HIS113 2.0 38.9 1.0 NE2 D:HIS113 2.2 45.2 1.0 SG D:CYS181 2.3 45.0 1.0 SG D:CYS110 2.3 47.0 1.0 O D:HOH3334 2.4 36.9 1.0 CB D:CYS181 3.1 34.6 1.0 CB D:CYS110 3.2 37.0 1.0 CG D:HIS113 3.3 34.3 1.0 CE1 D:HIS113 3.5 35.4 1.0 CB D:HIS112 3.6 38.9 1.0 N D:HIS113 4.0 30.0 1.0 ND1 D:HIS113 4.0 30.7 1.0 C D:HIS112 4.3 31.3 1.0 CA D:HIS112 4.3 32.2 1.0 CB D:HIS113 4.3 27.8 1.0 ND1 D:HIS112 4.3 54.8 1.0 CG D:HIS112 4.4 50.2 1.0 N D:HIS112 4.5 33.4 1.0 CA D:CYS181 4.5 37.3 1.0 CA D:CYS110 4.6 36.8 1.0 CA D:HIS113 4.8 28.8 1.0 C D:CYS110 4.9 37.0 1.0

Zinc binding site 5 out of 15 in the Crystal Structure of Zinc-Containing E.Coli Gtp Cyclohydrolase I


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Crystal Structure of Zinc-Containing E.Coli Gtp Cyclohydrolase I within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn3320 b:60.2 occ:1.00 CD2 E:HIS113 2.0 51.4 1.0 NE2 E:HIS113 2.2 54.1 1.0 SG E:CYS181 2.2 51.9 1.0 SG E:CYS110 2.3 51.9 1.0 O E:HOH3335 2.4 15.8 1.0 CB E:CYS181 2.9 37.4 1.0 CB E:CYS110 3.2 47.8 1.0 CG E:HIS113 3.3 47.8 1.0 CE1 E:HIS113 3.5 45.0 1.0 CB E:HIS112 3.6 53.0 1.0 ND1 E:HIS113 4.0 46.2 1.0 N E:HIS113 4.1 42.6 1.0 CB E:HIS113 4.3 43.5 1.0 ND1 E:HIS112 4.3 68.5 1.0 C E:HIS112 4.3 45.6 1.0 CA E:HIS112 4.4 47.7 1.0 CG E:HIS112 4.4 63.9 1.0 CA E:CYS181 4.4 39.3 1.0 N E:HIS112 4.5 50.6 1.0 CA E:CYS110 4.7 47.8 1.0 CA E:HIS113 4.8 43.3 1.0 C E:CYS110 5.0 48.4 1.0

Zinc binding site 6 out of 15 in the Crystal Structure of Zinc-Containing E.Coli Gtp Cyclohydrolase I


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Crystal Structure of Zinc-Containing E.Coli Gtp Cyclohydrolase I within 5.0Å range: probe atom residue distance (Å) B Occ F:Zn3321 b:58.1 occ:1.00 CD2 F:HIS113 2.0 46.6 1.0 SG F:CYS181 2.2 51.9 1.0 NE2 F:HIS113 2.2 49.1 1.0 SG F:CYS110 2.2 49.3 1.0 O F:HOH3336 2.3 30.1 1.0 CB F:CYS181 3.0 42.1 1.0 CB F:CYS110 3.1 42.0 1.0 CG F:HIS113 3.3 42.4 1.0 CE1 F:HIS113 3.5 41.2 1.0 CB F:HIS112 3.5 48.4 1.0 N F:HIS113 4.0 36.5 1.0 ND1 F:HIS113 4.0 38.9 1.0 ND1 F:HIS112 4.2 57.8 1.0 CB F:HIS113 4.2 37.2 1.0 CG F:HIS112 4.4 56.1 1.0 CA F:HIS112 4.4 41.1 1.0 C F:HIS112 4.4 38.4 1.0 CA F:CYS181 4.4 40.9 1.0 CA F:CYS110 4.6 40.8 1.0 N F:HIS112 4.6 42.2 1.0 CA F:HIS113 4.7 36.0 1.0 O F:CYS181 4.8 44.0 1.0 C F:CYS110 4.9 43.9 1.0 C F:CYS181 4.9 40.7 1.0 O F:CYS110 5.0 47.9 1.0

Zinc binding site 7 out of 15 in the Crystal Structure of Zinc-Containing E.Coli Gtp Cyclohydrolase I


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Crystal Structure of Zinc-Containing E.Coli Gtp Cyclohydrolase I within 5.0Å range: probe atom residue distance (Å) B Occ G:Zn3322 b:67.0 occ:1.00 CD2 G:HIS113 2.0 58.4 1.0 NE2 G:HIS113 2.2 60.9 1.0 SG G:CYS181 2.2 54.8 1.0 SG G:CYS110 2.3 56.8 1.0 O G:HOH3337 2.7 36.8 1.0 CB G:CYS181 3.1 48.1 1.0 CB G:CYS110 3.2 51.5 1.0 CG G:HIS113 3.3 54.1 1.0 CB G:HIS112 3.4 62.7 1.0 CE1 G:HIS113 3.5 53.5 1.0 N G:HIS113 4.0 55.8 1.0 ND1 G:HIS113 4.0 50.9 1.0 CA G:HIS112 4.2 59.1 1.0 C G:HIS112 4.3 57.4 1.0 CB G:HIS113 4.3 51.9 1.0 N G:HIS112 4.4 57.8 1.0 CG G:HIS112 4.5 71.6 1.0 ND1 G:HIS112 4.5 75.8 1.0 CA G:CYS181 4.5 47.5 1.0 CA G:CYS110 4.6 52.7 1.0 CA G:HIS113 4.8 54.0 1.0 C G:CYS110 4.9 53.1 1.0

Zinc binding site 8 out of 15 in the Crystal Structure of Zinc-Containing E.Coli Gtp Cyclohydrolase I


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Crystal Structure of Zinc-Containing E.Coli Gtp Cyclohydrolase I within 5.0Å range: probe atom residue distance (Å) B Occ H:Zn3323 b:58.9 occ:1.00 CD2 H:HIS113 1.9 44.3 1.0 NE2 H:HIS113 2.2 49.4 1.0 SG H:CYS110 2.2 47.9 1.0 SG H:CYS181 2.2 52.5 1.0 O H:HOH3338 2.4 31.6 1.0 CB H:CYS181 3.1 41.0 1.0 CB H:CYS110 3.1 38.9 1.0 CG H:HIS113 3.2 40.7 1.0 CE1 H:HIS113 3.5 41.7 1.0 CB H:HIS112 3.6 42.8 1.0 ND1 H:HIS113 3.9 38.6 1.0 N H:HIS113 4.0 34.9 1.0 CB H:HIS113 4.2 34.0 1.0 C H:HIS112 4.3 36.5 1.0 CA H:HIS112 4.3 36.6 1.0 N H:HIS112 4.4 35.7 1.0 ND1 H:HIS112 4.5 57.7 1.0 CA H:CYS110 4.5 40.2 1.0 CA H:CYS181 4.5 40.9 1.0 CG H:HIS112 4.5 53.2 1.0 CA H:HIS113 4.7 35.3 1.0 C H:CYS110 4.8 40.6 1.0 O H:HIS112 5.0 37.5 1.0 C H:CYS181 5.0 41.7 1.0

Zinc binding site 9 out of 15 in the Crystal Structure of Zinc-Containing E.Coli Gtp Cyclohydrolase I


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 9 of Crystal Structure of Zinc-Containing E.Coli Gtp Cyclohydrolase I within 5.0Å range: probe atom residue distance (Å) B Occ I:Zn3324 b:65.2 occ:1.00 CD2 I:HIS113 1.9 50.7 1.0 NE2 I:HIS113 2.2 56.3 1.0 SG I:CYS181 2.2 56.4 1.0 SG I:CYS110 2.3 57.5 1.0 O I:HOH3339 2.4 26.6 1.0 CB I:CYS181 2.9 47.0 1.0 CB I:CYS110 3.0 51.4 1.0 CG I:HIS113 3.2 49.2 1.0 CE1 I:HIS113 3.4 50.6 1.0 CB I:HIS112 3.7 55.2 1.0 ND1 I:HIS113 3.9 47.7 1.0 N I:HIS113 4.0 50.0 1.0 CB I:HIS113 4.2 48.2 1.0 C I:HIS112 4.3 50.2 1.0 CA I:HIS112 4.4 50.8 1.0 CA I:CYS181 4.4 46.3 1.0 CA I:CYS110 4.5 50.5 1.0 N I:HIS112 4.6 51.2 1.0 CG I:HIS112 4.7 63.9 1.0 CA I:HIS113 4.7 49.7 1.0 ND1 I:HIS112 4.8 68.2 1.0 C I:CYS110 4.9 52.1 1.0 N I:CYS181 5.0 43.9 1.0 O I:HIS112 5.0 50.9 1.0

Zinc binding site 10 out of 15 in the Crystal Structure of Zinc-Containing E.Coli Gtp Cyclohydrolase I


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 10 of Crystal Structure of Zinc-Containing E.Coli Gtp Cyclohydrolase I within 5.0Å range: probe atom residue distance (Å) B Occ J:Zn3325 b:57.7 occ:1.00 CD2 J:HIS113 2.0 54.3 1.0 NE2 J:HIS113 2.2 57.8 1.0 SG J:CYS181 2.2 54.0 1.0 SG J:CYS110 2.3 57.5 1.0 O J:HOH3340 2.5 45.0 1.0 CB J:CYS181 3.0 46.7 1.0 CB J:CYS110 3.1 53.9 1.0 CG J:HIS113 3.2 50.5 1.0 CE1 J:HIS113 3.5 51.9 1.0 CB J:HIS112 3.7 58.3 1.0 ND1 J:HIS113 4.0 49.6 1.0 N J:HIS113 4.1 51.5 1.0 CB J:HIS113 4.2 49.0 1.0 CA J:CYS181 4.4 44.8 1.0 ND1 J:HIS112 4.4 65.0 1.0 CA J:HIS112 4.5 55.3 1.0 C J:HIS112 4.5 54.0 1.0 CG J:HIS112 4.5 62.8 1.0 CA J:CYS110 4.5 54.2 1.0 N J:HIS112 4.7 55.6 1.0 CA J:HIS113 4.8 48.6 1.0 C J:CYS110 4.9 56.2 1.0 N J:CYS181 4.9 43.4 1.0 O J:CYS110 4.9 58.5 1.0 C J:CYS181 5.0 43.4 1.0

G.Auerbach, A.Herrmann, A.Bracher, G.Bader, M.Gutlich, M.Fischer, M.Neukamm, M.Garrido-Franco, J.Richardson, H.Nar, R.Huber, A.Bacher. Zinc Plays A Key Role in Human and Bacterial Gtp Cyclohydrolase I. Proc.Natl.Acad.Sci.Usa V. 97 13567 2000.
ISSN: ISSN 0027-8424
PubMed: 11087827
DOI: 10.1073/PNAS.240463497