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Zinc in PDB 2fpu: Crystal Structure of the N-Terminal Domain of E.Coli Hisb- Complex with Histidinol

Enzymatic activity of Crystal Structure of the N-Terminal Domain of E.Coli Hisb- Complex with Histidinol

All present enzymatic activity of Crystal Structure of the N-Terminal Domain of E.Coli Hisb- Complex with Histidinol:
3.1.3.15;

Protein crystallography data

The structure of Crystal Structure of the N-Terminal Domain of E.Coli Hisb- Complex with Histidinol, PDB code: 2fpu was solved by E.S.Rangarajan, M.Cygler, A.Matte, Montreal-Kingston Bacterialstructural Genomics Initiative (Bsgi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.80
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 53.502, 132.664, 107.313, 90.00, 90.00, 90.00
R / Rfree (%) 18.3 / 22.3

Other elements in 2fpu:

The structure of Crystal Structure of the N-Terminal Domain of E.Coli Hisb- Complex with Histidinol also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms
Chlorine (Cl) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the N-Terminal Domain of E.Coli Hisb- Complex with Histidinol (pdb code 2fpu). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the N-Terminal Domain of E.Coli Hisb- Complex with Histidinol, PDB code: 2fpu:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2fpu

Go back to Zinc Binding Sites List in 2fpu
Zinc binding site 1 out of 2 in the Crystal Structure of the N-Terminal Domain of E.Coli Hisb- Complex with Histidinol


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 the N-Terminal Domain of E.Coli Hisb- Complex with Histidinol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn506

b:29.4
occ:1.00
ND1 A:HIS96 2.1 26.8 1.0
SG A:CYS104 2.2 27.4 1.0
SG A:CYS94 2.3 24.0 1.0
SG A:CYS102 2.4 32.0 1.0
CE1 A:HIS96 3.0 27.8 1.0
CG A:HIS96 3.1 27.3 1.0
CB A:CYS102 3.3 32.8 1.0
CB A:CYS94 3.4 24.3 1.0
CB A:CYS104 3.5 27.2 1.0
CB A:HIS96 3.5 27.2 1.0
N A:ARG105 3.6 25.5 1.0
C A:CYS104 3.8 26.5 1.0
N A:CYS104 3.8 28.5 1.0
CA A:CYS104 3.8 27.3 1.0
CA A:CYS94 4.1 24.0 1.0
NE2 A:HIS96 4.1 27.4 1.0
N A:HIS96 4.2 26.5 1.0
CD2 A:HIS96 4.2 28.0 1.0
CA A:ARG105 4.3 24.7 1.0
CD A:PRO95 4.4 24.4 1.0
CB A:ARG105 4.4 24.9 1.0
O A:HOH678 4.5 43.5 1.0
CA A:HIS96 4.5 27.4 1.0
O A:CYS104 4.5 26.4 1.0
C A:CYS94 4.5 24.1 1.0
O A:HOH573 4.5 28.0 1.0
N A:PRO95 4.6 24.3 1.0
CA A:CYS102 4.7 32.6 1.0
N A:ASP103 4.8 31.1 1.0
C A:CYS102 4.9 32.1 1.0
O A:HOH597 5.0 34.1 1.0

Zinc binding site 2 out of 2 in 2fpu

Go back to Zinc Binding Sites List in 2fpu
Zinc binding site 2 out of 2 in the Crystal Structure of the N-Terminal Domain of E.Coli Hisb- Complex with Histidinol


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 the N-Terminal Domain of E.Coli Hisb- Complex with Histidinol within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn505

b:15.4
occ:1.00
ND1 B:HIS96 2.1 14.2 1.0
SG B:CYS102 2.3 13.6 1.0
SG B:CYS94 2.3 11.9 1.0
SG B:CYS104 2.3 14.8 1.0
CE1 B:HIS96 3.1 14.6 1.0
CG B:HIS96 3.1 13.2 1.0
CB B:CYS102 3.2 14.1 1.0
CB B:HIS96 3.4 13.6 1.0
CB B:CYS94 3.5 12.8 1.0
N B:ARG105 3.5 13.1 1.0
CB B:CYS104 3.5 13.5 1.0
C B:CYS104 3.7 13.5 1.0
CA B:CYS104 3.8 13.5 1.0
N B:CYS104 3.8 13.6 1.0
CA B:CYS94 4.1 12.5 1.0
N B:HIS96 4.2 13.9 1.0
CA B:ARG105 4.2 13.1 1.0
NE2 B:HIS96 4.2 13.9 1.0
CD2 B:HIS96 4.2 13.9 1.0
CB B:ARG105 4.3 13.4 1.0
CD B:PRO95 4.3 13.3 1.0
CA B:HIS96 4.4 14.0 1.0
O B:CYS104 4.5 12.9 1.0
O B:HOH534 4.5 25.3 1.0
C B:CYS94 4.6 12.3 1.0
CA B:CYS102 4.6 14.0 1.0
N B:PRO95 4.6 12.2 1.0
C B:CYS102 4.8 13.8 1.0
N B:ASP103 4.9 14.1 1.0
O B:HOH662 5.0 27.2 1.0

Reference:

E.S.Rangarajan, A.Proteau, J.Wagner, M.N.Hung, A.Matte, M.Cygler. Structural Snapshots of Escherichia Coli Histidinol Phosphate Phosphatase Along the Reaction Pathway. J.Biol.Chem. V. 281 37930 2006.
ISSN: ISSN 0021-9258
PubMed: 16966333
DOI: 10.1074/JBC.M604916200
Page generated: Wed Dec 16 03:28:33 2020

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