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Chlorine 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
Zinc (Zn) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine 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 Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Crystal Structure of the N-Terminal Domain of E.Coli Hisb- Complex with Histidinol, PDB code: 2fpu:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in 2fpu

Go back to Chlorine Binding Sites List in 2fpu
Chlorine binding site 1 out of 4 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 Chlorine with other atoms in the Cl 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:Cl502

b:21.5
occ:1.00
 O A:HOH523 3.0 17.8 1.0
O A:HOH567 3.0 20.0 1.0
O A:HOH519 3.2 18.6 1.0
NZ A:LYS106 3.3 19.7 1.0
O A:HOH512 3.3 13.9 1.0
CE A:LYS106 3.4 21.7 1.0
OD1 A:ASP10 3.4 13.0 1.0
N A:ASN56 3.6 17.7 1.0
CB A:ASN56 3.7 18.1 1.0
O A:HOH514 3.9 18.3 1.0
O A:HOH533 3.9 20.5 1.0
ND2 A:ASN56 4.1 19.8 1.0
CG A:ASN56 4.1 18.9 1.0
CA A:ASN56 4.2 18.3 1.0
O A:HOH555 4.2 23.0 1.0
O A:ASN56 4.2 18.4 1.0
CG A:ASP10 4.3 14.3 1.0
MG A:MG507 4.5 15.8 1.0
OD1 A:ASP135 4.5 16.4 1.0
C A:THR55 4.6 18.1 1.0
OD2 A:ASP10 4.7 14.5 1.0
CA A:THR55 4.7 18.2 1.0
C A:ASN56 4.7 18.1 1.0
CD A:LYS106 4.8 22.5 1.0
OD1 A:ASN56 4.9 19.9 1.0
OG1 A:THR55 5.0 18.8 1.0
CD A:ARG132 5.0 17.7 1.0

Chlorine binding site 2 out of 4 in 2fpu

Go back to Chlorine Binding Sites List in 2fpu
Chlorine binding site 2 out of 4 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 Chlorine with other atoms in the Cl 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:Cl501

b:17.6
occ:1.00
 NZ B:LYS106 3.1 9.9 1.0
O B:HOH600 3.1 20.0 1.0
O B:HOH681 3.2 42.0 1.0
O B:HOH609 3.2 17.5 1.0
N B:ASN56 3.4 12.3 1.0
OD1 B:ASP10 3.5 9.6 1.0
CB B:ASN56 3.6 12.1 1.0
O B:HSO509 3.7 18.3 1.0
C B:HSO509 3.7 19.9 1.0
CD B:LYS106 3.7 12.6 1.0
O B:HOH521 3.8 17.9 1.0
CE B:LYS106 3.8 11.7 1.0
O B:HOH791 3.9 14.9 1.0
ND2 B:ASN56 3.9 12.1 1.0
CG B:ASN56 4.0 12.7 1.0
CA B:ASN56 4.1 12.3 1.0
O B:ASN56 4.2 12.2 1.0
C B:THR55 4.4 12.6 1.0
CA B:THR55 4.5 12.9 1.0
CG B:ASP10 4.5 11.4 1.0
C B:ASN56 4.6 12.4 1.0
OG1 B:THR55 4.7 13.6 1.0
OD1 B:ASP135 4.7 14.5 1.0
MG B:MG508 4.7 12.6 1.0
OD1 B:ASN56 4.8 12.7 1.0
OD2 B:ASP10 4.9 9.8 1.0

Chlorine binding site 3 out of 4 in 2fpu

Go back to Chlorine Binding Sites List in 2fpu
Chlorine binding site 3 out of 4 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 Chlorine with other atoms in the Cl binding site number 3 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:Cl503

b:25.2
occ:1.00
 OG B:SER21 2.8 12.6 1.0
N B:SER21 3.3 12.3 1.0
CB B:SER21 3.4 12.5 1.0
CD B:PRO20 3.4 11.2 1.0
N B:PRO20 3.7 11.4 1.0
CB B:PRO19 3.8 11.5 1.0
CG B:PRO20 3.8 10.6 1.0
O B:HOH608 3.9 25.1 1.0
CA B:SER21 4.0 12.8 1.0
C B:PRO19 4.0 11.1 1.0
CA B:PRO19 4.0 11.5 1.0
C B:PRO20 4.3 11.7 1.0
CA B:PRO20 4.4 11.2 1.0
CB B:PRO20 4.8 10.9 1.0
O B:PRO19 4.8 11.6 1.0
CE B:LYS30 4.8 16.4 1.0

Chlorine binding site 4 out of 4 in 2fpu

Go back to Chlorine Binding Sites List in 2fpu
Chlorine binding site 4 out of 4 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 Chlorine with other atoms in the Cl binding site number 4 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:Cl504

b:28.7
occ:1.00
 O B:VAL25 2.8 11.3 1.0
O B:PHE70 2.9 12.5 1.0
NH1 B:ARG11 3.0 9.6 1.0
NH2 B:ARG11 3.1 12.2 1.0
CD1 B:PHE70 3.4 13.9 1.0
N B:HIS74 3.5 11.1 1.0
CZ B:ARG11 3.5 11.6 1.0
C B:PHE70 3.7 12.9 1.0
CB B:PRO73 3.7 12.7 1.0
CA B:PHE70 3.8 13.0 1.0
CB B:HIS74 3.8 11.7 1.0
CE1 B:PHE70 3.8 12.9 1.0
CG B:PHE70 3.8 13.1 1.0
CB B:VAL25 3.9 12.2 1.0
C B:VAL25 4.0 12.3 1.0
CA B:HIS74 4.0 11.8 1.0
C B:PRO73 4.2 11.9 1.0
CG1 B:VAL25 4.2 12.6 1.0
CB B:PHE70 4.3 12.7 1.0
CG B:PRO73 4.4 11.9 1.0
CA B:PRO73 4.5 11.7 1.0
CZ B:PHE70 4.5 11.8 1.0
CA B:VAL25 4.5 11.8 1.0
CD B:PRO73 4.6 11.5 1.0
CD2 B:PHE70 4.6 12.9 1.0
N B:PRO73 4.8 12.0 1.0
NE B:ARG11 4.9 11.5 1.0
O B:ASP69 4.9 13.2 1.0
CG B:HIS74 4.9 12.2 1.0
CE2 B:PHE70 4.9 13.1 1.0
CZ B:PHE65 4.9 16.2 1.0
O B:HOH511 4.9 11.4 1.0
N B:ASP71 5.0 12.5 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: Sat Jul 20 07:11:24 2024

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