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Zinc in PDB 2fpw: Crystal Structure of the N-Terminal Domain of E.Coli Hisb- Phosphoaspartate Intermediate.

Enzymatic activity of Crystal Structure of the N-Terminal Domain of E.Coli Hisb- Phosphoaspartate Intermediate.

All present enzymatic activity of Crystal Structure of the N-Terminal Domain of E.Coli Hisb- Phosphoaspartate Intermediate.:
3.1.3.15;

Protein crystallography data

The structure of Crystal Structure of the N-Terminal Domain of E.Coli Hisb- Phosphoaspartate Intermediate., PDB code: 2fpw 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 / 1.75
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 52.983, 132.408, 105.685, 90.00, 90.00, 90.00
R / Rfree (%) 17.8 / 21.1

Other elements in 2fpw:

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

Calcium (Ca) 3 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the N-Terminal Domain of E.Coli Hisb- Phosphoaspartate Intermediate. (pdb code 2fpw). 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- Phosphoaspartate Intermediate., PDB code: 2fpw:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2fpw

Go back to Zinc Binding Sites List in 2fpw
Zinc binding site 1 out of 2 in the Crystal Structure of the N-Terminal Domain of E.Coli Hisb- Phosphoaspartate Intermediate.


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- Phosphoaspartate Intermediate. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn502

b:26.1
occ:1.00
ND1 A:HIS96 2.1 25.7 1.0
SG A:CYS104 2.2 25.6 1.0
SG A:CYS94 2.3 20.1 1.0
SG A:CYS102 2.4 29.2 1.0
CE1 A:HIS96 3.0 26.1 1.0
CG A:HIS96 3.1 25.5 1.0
CB A:CYS102 3.3 31.1 1.0
CB A:CYS94 3.4 20.7 1.0
CB A:HIS96 3.5 24.7 1.0
CB A:CYS104 3.5 26.0 1.0
N A:ARG105 3.6 24.2 1.0
C A:CYS104 3.7 25.5 1.0
N A:CYS104 3.7 27.4 1.0
CA A:CYS104 3.8 26.1 1.0
CA A:CYS94 4.1 20.6 1.0
NE2 A:HIS96 4.1 26.5 1.0
N A:HIS96 4.2 23.8 1.0
CD2 A:HIS96 4.2 26.8 1.0
CA A:ARG105 4.3 23.4 1.0
CD A:PRO95 4.3 21.8 1.0
O A:CYS104 4.4 25.3 1.0
CA A:HIS96 4.4 24.8 1.0
CB A:ARG105 4.5 23.8 1.0
C A:CYS94 4.5 21.1 1.0
N A:PRO95 4.5 21.6 1.0
O A:HOH572 4.6 25.7 1.0
CA A:CYS102 4.7 31.0 1.0
N A:ASP103 4.9 30.1 1.0
C A:CYS102 4.9 30.6 1.0
C A:ASP103 5.0 28.9 1.0

Zinc binding site 2 out of 2 in 2fpw

Go back to Zinc Binding Sites List in 2fpw
Zinc binding site 2 out of 2 in the Crystal Structure of the N-Terminal Domain of E.Coli Hisb- Phosphoaspartate Intermediate.


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- Phosphoaspartate Intermediate. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn501

b:14.2
occ:1.00
ND1 B:HIS96 2.1 11.7 1.0
SG B:CYS102 2.3 15.6 1.0
SG B:CYS94 2.3 11.5 1.0
SG B:CYS104 2.3 12.1 1.0
CE1 B:HIS96 3.1 11.7 1.0
CG B:HIS96 3.1 11.8 1.0
CB B:CYS102 3.2 15.2 1.0
CB B:CYS94 3.4 11.2 1.0
CB B:HIS96 3.4 12.9 1.0
CB B:CYS104 3.5 13.0 1.0
N B:ARG105 3.5 12.7 1.0
C B:CYS104 3.8 12.8 1.0
CA B:CYS104 3.8 12.8 1.0
N B:CYS104 3.8 13.3 1.0
CA B:CYS94 4.0 11.5 1.0
NE2 B:HIS96 4.2 10.2 1.0
N B:HIS96 4.2 12.7 1.0
CD2 B:HIS96 4.2 11.2 1.0
CA B:ARG105 4.2 12.0 1.0
CD B:PRO95 4.3 12.3 1.0
CB B:ARG105 4.3 12.2 1.0
CA B:HIS96 4.5 13.2 1.0
C B:CYS94 4.5 11.7 1.0
O B:CYS104 4.5 12.5 1.0
N B:PRO95 4.5 11.9 1.0
O B:HOH523 4.5 15.8 1.0
CA B:CYS102 4.6 15.4 1.0
C B:CYS102 4.8 14.8 1.0
N B:ASP103 4.9 14.3 1.0
O B:HOH607 4.9 20.8 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 03:28:34 2020

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