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Chlorine in PDB 9bpw: Crystal Structure of Fumarate Hydratase Fumc From Staphylococcus Aureus

Enzymatic activity of Crystal Structure of Fumarate Hydratase Fumc From Staphylococcus Aureus

All present enzymatic activity of Crystal Structure of Fumarate Hydratase Fumc From Staphylococcus Aureus:
4.2.1.2;

Protein crystallography data

The structure of Crystal Structure of Fumarate Hydratase Fumc From Staphylococcus Aureus, PDB code: 9bpw was solved by Y.Kim, C.Tesar, M.Endres, G.Babnigg, T.Wong, A.Joachimiak, Center Forstructural Biology Of Infectious Diseases (Csbid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.73 / 2.00
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 243.865, 108.891, 109.023, 90, 116.62, 90
R / Rfree (%) 18.4 / 21.5

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Fumarate Hydratase Fumc From Staphylococcus Aureus (pdb code 9bpw). 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 Fumarate Hydratase Fumc From Staphylococcus Aureus, PDB code: 9bpw:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in 9bpw

Go back to Chlorine Binding Sites List in 9bpw
Chlorine binding site 1 out of 4 in the Crystal Structure of Fumarate Hydratase Fumc From Staphylococcus Aureus


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 Fumarate Hydratase Fumc From Staphylococcus Aureus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl507

b:76.3
occ:1.00
O B:HOH734 2.7 47.6 1.0
NH1 A:ARG203 3.6 41.5 1.0
NH2 A:ARG203 3.7 42.3 1.0
CZ A:ARG203 4.1 43.9 1.0
O A:HOH718 4.4 47.2 1.0
CE1 A:TYR204 4.8 41.7 1.0
CD1 A:TYR204 4.8 42.6 1.0

Chlorine binding site 2 out of 4 in 9bpw

Go back to Chlorine Binding Sites List in 9bpw
Chlorine binding site 2 out of 4 in the Crystal Structure of Fumarate Hydratase Fumc From Staphylococcus Aureus


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 Fumarate Hydratase Fumc From Staphylococcus Aureus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl508

b:79.6
occ:1.00
NH2 A:ARG166 3.3 48.5 1.0
NH1 A:ARG166 3.7 49.3 1.0
CZ A:ARG166 4.0 48.3 1.0
CE A:LYS170 4.2 49.4 1.0
CG A:LYS170 4.8 43.0 1.0
CD A:LYS170 4.9 45.6 1.0

Chlorine binding site 3 out of 4 in 9bpw

Go back to Chlorine Binding Sites List in 9bpw
Chlorine binding site 3 out of 4 in the Crystal Structure of Fumarate Hydratase Fumc From Staphylococcus Aureus


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 Fumarate Hydratase Fumc From Staphylococcus Aureus within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl507

b:81.8
occ:1.00
O A:HOH722 3.0 44.8 1.0
NH1 B:ARG203 3.6 43.5 1.0
NH2 B:ARG203 3.9 42.5 1.0
CZ B:ARG203 4.2 43.6 1.0
O B:HOH708 4.3 45.6 1.0
CG A:GLU260 4.4 63.3 1.0
CE1 B:TYR204 4.7 44.0 1.0
CD1 B:TYR204 4.8 41.0 1.0
O A:GLU260 5.0 48.3 1.0

Chlorine binding site 4 out of 4 in 9bpw

Go back to Chlorine Binding Sites List in 9bpw
Chlorine binding site 4 out of 4 in the Crystal Structure of Fumarate Hydratase Fumc From Staphylococcus Aureus


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 Fumarate Hydratase Fumc From Staphylococcus Aureus within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl508

b:82.3
occ:1.00
NH2 C:ARG166 3.3 48.9 1.0
NH1 C:ARG166 3.4 48.7 1.0
CZ C:ARG166 3.8 45.1 1.0
CE C:LYS170 3.9 48.5 1.0
CG C:LYS170 4.5 45.4 1.0
CD C:LYS170 4.6 46.8 1.0
NZ C:LYS170 4.7 55.0 1.0

Reference:

Y.Kim, C.Tesar, M.Endres, G.Babnigg, T.Wong, A.Joachimiak, Center For Structural Biology Of Infectious Diseases (Csbid). Crystal Structure of Fumarate Hydratase Fumc From Staphylococcus Aureus To Be Published.
Page generated: Sun Jul 13 16:06:01 2025

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