Zinc in PDB 1fb1: Crystal Structure of Human Gtp Cyclohydrolase I

All present enzymatic activity of Crystal Structure of Human Gtp Cyclohydrolase I:
3.5.4.16;

The structure of Crystal Structure of Human Gtp Cyclohydrolase I, PDB code: 1fb1 was solved by G.Auerbach, A.Herrmann, A.Bracher, G.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)	14.97 / 3.10
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	115.110, 115.110, 387.310, 90.00, 90.00, 120.00
R / Rfree (%)	20.4 / 29.3

The binding sites of Zinc atom in the Crystal Structure of Human Gtp Cyclohydrolase I (pdb code 1fb1). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 5 binding sites of Zinc where determined in the Crystal Structure of Human Gtp Cyclohydrolase I, PDB code: 1fb1:
Jump to Zinc binding site number: 1; 2; 3; 4; 5;

Zinc binding site 1 out of 5 in the Crystal Structure of Human 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 Human Gtp Cyclohydrolase I within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn300 b:0.9 occ:1.00 NE2 A:HIS144 2.2 87.7 1.0 SG A:CYS212 2.2 95.8 1.0 SG A:CYS141 2.2 86.1 1.0 CD2 A:HIS144 2.4 78.6 1.0 O2 B:IPA302 2.7 65.5 1.0 CB A:CYS212 3.1 95.2 1.0 CB A:CYS141 3.2 68.7 1.0 C3 B:IPA302 3.3 67.1 1.0 CE1 A:HIS144 3.4 81.5 1.0 C2 B:IPA302 3.6 67.9 1.0 CG A:HIS144 3.7 74.0 1.0 ND1 A:HIS144 4.1 74.2 1.0 N A:HIS144 4.5 70.0 1.0 CB A:HIS143 4.5 79.5 1.0 CA A:CYS141 4.6 65.2 1.0 CA A:CYS212 4.6 95.3 1.0 C1 B:IPA302 4.7 64.8 1.0 CB A:HIS144 4.8 68.6 1.0 ND1 A:HIS210 5.0 76.2 1.0

Zinc binding site 2 out of 5 in the Crystal Structure of Human 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 Human Gtp Cyclohydrolase I within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn300 b:0.7 occ:1.00 NE2 B:HIS144 2.2 92.1 1.0 O2 B:IPA303 2.2 51.9 1.0 SG B:CYS212 2.2 0.0 1.0 CD2 B:HIS144 2.2 82.8 1.0 SG B:CYS141 2.2 88.8 1.0 C2 B:IPA303 3.4 54.6 1.0 CB B:CYS212 3.4 0.8 1.0 CB B:CYS141 3.5 74.9 1.0 CE1 B:HIS144 3.5 85.1 1.0 CG B:HIS144 3.6 79.6 1.0 C3 B:IPA303 3.7 49.1 1.0 C1 B:IPA303 3.9 58.7 1.0 ND1 B:HIS144 4.2 80.8 1.0 CB B:HIS143 4.4 55.7 1.0 OG C:SER166 4.4 81.7 1.0 N B:HIS144 4.7 60.1 1.0 CB B:HIS144 4.7 71.2 1.0 ND1 B:HIS210 4.8 86.6 1.0 CA B:CYS212 4.8 0.7 1.0 ND1 B:HIS143 4.8 62.6 1.0 CA B:CYS141 4.8 71.5 1.0

Zinc binding site 3 out of 5 in the Crystal Structure of Human 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 Human Gtp Cyclohydrolase I within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn300 b:0.2 occ:1.00 NE2 C:HIS144 2.1 0.1 1.0 CD2 C:HIS144 2.1 0.6 1.0 SG C:CYS141 2.2 0.6 1.0 SG C:CYS212 2.3 0.5 1.0 O2 D:IPA304 2.5 78.6 1.0 CB C:CYS212 2.9 1.0 1.0 C2 D:IPA304 3.1 77.6 1.0 CB C:CYS141 3.4 0.7 1.0 CE1 C:HIS144 3.4 0.7 1.0 CG C:HIS144 3.5 0.7 1.0 C1 D:IPA304 3.8 76.6 1.0 ND1 C:HIS144 4.0 0.5 1.0 CA C:CYS212 4.4 0.4 1.0 C3 D:IPA304 4.4 76.5 1.0 CB C:HIS144 4.6 0.4 1.0 CB C:HIS143 4.7 99.2 1.0 CA C:CYS141 4.8 0.4 1.0 N C:CYS212 4.8 0.7 1.0 N C:HIS144 4.9 0.6 1.0

Zinc binding site 4 out of 5 in the Crystal Structure of Human 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 Human Gtp Cyclohydrolase I within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn300 b:1.0 occ:1.00 NE2 D:HIS144 2.2 92.9 1.0 SG D:CYS212 2.3 0.5 1.0 SG D:CYS141 2.3 89.5 1.0 CD2 D:HIS144 2.3 89.2 1.0 O2 D:IPA305 2.7 63.8 1.0 CB D:CYS212 3.1 99.3 1.0 CE1 D:HIS144 3.4 89.2 1.0 CB D:CYS141 3.4 76.2 1.0 CG D:HIS144 3.6 83.9 1.0 C2 D:IPA305 3.7 62.5 1.0 C3 D:IPA305 4.1 60.8 1.0 ND1 D:HIS144 4.1 86.2 1.0 C1 D:IPA305 4.1 61.2 1.0 CB D:HIS143 4.3 85.0 1.0 N D:HIS144 4.5 77.6 1.0 CA D:CYS212 4.5 99.9 1.0 CB D:HIS144 4.6 78.7 1.0 CA D:CYS141 4.8 76.0 1.0 N D:CYS212 4.9 97.0 1.0

Zinc binding site 5 out of 5 in the Crystal Structure of Human 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 Human Gtp Cyclohydrolase I within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn300 b:99.2 occ:1.00 NE2 E:HIS144 2.1 83.3 1.0 SG E:CYS141 2.2 80.9 1.0 SG E:CYS212 2.2 84.8 1.0 CD2 E:HIS144 2.2 77.0 1.0 O2 A:IPA306 2.3 52.1 1.0 CB E:CYS212 3.0 82.1 1.0 C2 A:IPA306 3.4 46.1 1.0 C1 A:IPA306 3.4 42.5 1.0 CB E:CYS141 3.4 69.0 1.0 CE1 E:HIS144 3.5 77.8 1.0 CG E:HIS144 3.6 75.3 1.0 C3 A:IPA306 4.1 41.0 1.0 ND1 E:HIS144 4.1 75.3 1.0 CA E:CYS212 4.4 80.6 1.0 CB E:HIS143 4.6 56.6 1.0 N E:HIS144 4.7 65.1 1.0 CB E:HIS144 4.7 69.8 1.0 CA E:CYS141 4.8 66.5 1.0 OG A:SER166 4.8 70.9 0.0 N E:CYS212 5.0 75.9 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