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

Enzymatic activity of 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;

Protein crystallography data

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

Other elements in 1fbx:

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

Zinc (Zn) 15 atoms

Chlorine Binding Sites:

Pages:

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

Binding sites:

The binding sites of Chlorine 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 Chlorine atom.
In total 15 binding sites of Chlorine where determined in the Crystal Structure of Zinc-Containing E.Coli Gtp Cyclohydrolase I, PDB code: 1fbx:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Chlorine binding site 1 out of 15 in 1fbx

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Chlorine 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 Chlorine with other atoms in the Cl 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:Cl3350

b:39.9
occ:1.00
 NH1 A:ARG139 2.7 42.0 1.0
NH2 E:ARG185 2.9 34.0 1.0
OG A:SER135 3.2 49.9 1.0
NZ A:LYS136 3.7 44.9 1.0
CZ A:ARG139 4.0 42.5 1.0
CZ E:ARG185 4.2 35.8 1.0
CB A:SER135 4.2 44.2 1.0
CE A:LYS136 4.5 44.5 1.0
NH2 A:ARG139 4.8 39.0 1.0
NE E:ARG185 4.8 37.2 1.0
CD A:ARG139 4.9 37.4 1.0
NE A:ARG139 4.9 39.3 1.0

Chlorine binding site 2 out of 15 in 1fbx

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Chlorine 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 Chlorine with other atoms in the Cl 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:Cl3346

b:27.9
occ:1.00
 NH2 A:ARG185 3.1 30.7 1.0
NH1 B:ARG139 3.2 32.3 1.0
NZ B:LYS136 3.2 44.7 1.0
OG B:SER135 3.4 34.6 1.0
CB B:SER135 4.3 31.6 1.0
CZ A:ARG185 4.4 30.2 1.0
CE B:LYS136 4.5 44.2 1.0
CZ B:ARG139 4.5 32.9 1.0

Chlorine binding site 3 out of 15 in 1fbx

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Chlorine 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 Chlorine with other atoms in the Cl 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:Cl3347

b:25.1
occ:1.00
 NH1 C:ARG139 2.9 32.4 1.0
OG C:SER135 3.3 38.1 1.0
NH2 B:ARG185 3.3 33.4 1.0
NZ C:LYS136 3.6 40.9 1.0
CZ C:ARG139 4.2 33.8 1.0
CB C:SER135 4.2 29.5 1.0
CE C:LYS136 4.3 37.1 1.0
CZ B:ARG185 4.6 28.3 1.0
NH2 C:ARG139 4.9 35.0 1.0
CE1 B:HIS113 4.9 33.6 1.0

Chlorine binding site 4 out of 15 in 1fbx

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Chlorine 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 Chlorine with other atoms in the Cl 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:Cl3348

b:27.2
occ:1.00
 NH1 D:ARG139 2.7 31.7 1.0
NH2 C:ARG185 3.1 39.8 1.0
OG D:SER135 3.3 33.7 1.0
NZ D:LYS136 3.7 36.7 1.0
CZ D:ARG139 4.0 32.9 1.0
CB D:SER135 4.3 30.2 1.0
CZ C:ARG185 4.4 38.2 1.0
CE D:LYS136 4.6 33.8 1.0
NH2 D:ARG139 4.7 33.8 1.0
CE1 C:HIS113 4.8 32.8 1.0
NE D:ARG139 5.0 27.3 1.0

Chlorine binding site 5 out of 15 in 1fbx

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Chlorine 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 Chlorine with other atoms in the Cl 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:Cl3349

b:28.8
occ:1.00
 NH1 E:ARG139 2.7 39.3 1.0
NH2 D:ARG185 2.9 47.4 1.0
NZ E:LYS136 3.2 38.2 1.0
OG E:SER135 3.2 47.5 1.0
CZ E:ARG139 4.0 39.2 1.0
CB E:SER135 4.1 42.5 1.0
CZ D:ARG185 4.2 44.9 1.0
CE E:LYS136 4.3 37.6 1.0
NH2 E:ARG139 4.8 33.7 1.0
CD E:ARG139 4.9 40.3 1.0
NE E:ARG139 4.9 40.3 1.0
NH1 D:ARG185 5.0 46.3 1.0

Chlorine binding site 6 out of 15 in 1fbx

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Chlorine 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 Chlorine with other atoms in the Cl 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:Cl3355

b:39.7
occ:1.00
 NZ F:LYS136 2.8 39.3 1.0
NH1 F:ARG139 2.9 46.9 1.0
NH2 J:ARG185 3.1 57.1 1.0
OG F:SER135 3.5 50.3 1.0
CE F:LYS136 4.2 41.2 1.0
CZ F:ARG139 4.2 45.0 1.0
CB F:SER135 4.3 44.3 1.0
CZ J:ARG185 4.4 55.0 1.0
NH2 F:ARG139 4.8 45.8 1.0

Chlorine binding site 7 out of 15 in 1fbx

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Chlorine 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 Chlorine with other atoms in the Cl 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:Cl3351

b:38.4
occ:1.00
 NH2 F:ARG185 2.9 47.0 1.0
NZ G:LYS136 3.2 51.8 1.0
OG G:SER135 3.3 50.1 1.0
NH1 G:ARG139 3.3 52.0 1.0
CB G:SER135 4.2 45.3 1.0
CZ F:ARG185 4.2 44.8 1.0
CZ G:ARG139 4.3 53.2 1.0
NH2 G:ARG139 4.4 50.1 1.0
CE G:LYS136 4.4 51.0 1.0
NH1 F:ARG185 5.0 44.5 1.0

Chlorine binding site 8 out of 15 in 1fbx

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Chlorine 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 Chlorine with other atoms in the Cl 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:Cl3352

b:42.8
occ:1.00
 NH1 H:ARG139 2.9 42.5 1.0
OG H:SER135 3.3 44.7 1.0
NH2 G:ARG185 3.3 44.4 1.0
NZ H:LYS136 3.5 43.0 1.0
CB H:SER135 4.2 44.8 1.0
CZ H:ARG139 4.2 43.8 1.0
CE H:LYS136 4.5 43.3 1.0
CZ G:ARG185 4.7 45.0 1.0
NH2 H:ARG139 4.8 45.9 1.0

Chlorine binding site 9 out of 15 in 1fbx

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Chlorine 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 Chlorine with other atoms in the Cl 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:Cl3353

b:29.6
occ:1.00
 NH1 I:ARG139 2.6 45.0 1.0
NH2 H:ARG185 3.1 34.5 1.0
OG I:SER135 3.3 44.2 1.0
NZ I:LYS136 3.5 45.3 1.0
CZ I:ARG139 3.9 46.0 1.0
CE I:LYS136 4.3 41.2 1.0
CB I:SER135 4.4 40.2 1.0
CZ H:ARG185 4.4 32.3 1.0
NH2 I:ARG139 4.5 47.1 1.0
NE I:ARG139 4.9 43.5 1.0

Chlorine binding site 10 out of 15 in 1fbx

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Chlorine 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 Chlorine with other atoms in the Cl 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:Cl3354

b:42.3
occ:1.00
 NH2 I:ARG185 2.8 48.2 1.0
NH1 J:ARG139 2.9 44.6 1.0
OG J:SER135 3.1 41.6 1.0
NZ J:LYS136 3.3 54.8 1.0
CB J:SER135 4.0 35.9 1.0
CZ I:ARG185 4.1 47.0 1.0
CZ J:ARG139 4.2 44.9 1.0
CE J:LYS136 4.2 50.4 1.0
NH2 J:ARG139 4.8 44.3 1.0
NE I:ARG185 4.9 44.3 1.0
NH1 I:ARG185 4.9 45.2 1.0

Reference:

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
Page generated: Sat Dec 12 08:35:16 2020

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