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Bromine in PDB 1n9k: Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution

Enzymatic activity of Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution

All present enzymatic activity of Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution:
3.1.3.2;

Protein crystallography data

The structure of Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution, PDB code: 1n9k was solved by V.Calderone, C.Forleo, M.Benvenuti, G.M.Rossolini, M.C.Thaller, S.Mangani, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.32 / 2.20
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 49.499, 92.616, 138.247, 90.00, 90.00, 90.00
R / Rfree (%) 18.9 / 23.1

Other elements in 1n9k:

The structure of Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Bromine Binding Sites:

Pages:

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

Binding sites:

The binding sites of Bromine atom in the Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution (pdb code 1n9k). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 15 binding sites of Bromine where determined in the Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution, PDB code: 1n9k:
Jump to Bromine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Bromine binding site 1 out of 15 in 1n9k

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Bromine binding site 1 out of 15 in the Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br213

b:34.2
occ:0.50
 O A:HOH1254 3.1 24.2 1.0
N A:LEU196 3.2 18.7 1.0
CA A:PRO195 3.7 19.9 1.0
CB A:PRO195 3.7 19.7 1.0
CG A:LEU196 3.8 17.4 1.0
CB A:LEU196 3.9 16.6 1.0
C A:PRO195 4.0 19.5 1.0
CD A:LYS194 4.1 18.8 1.0
CA A:LEU196 4.2 17.2 1.0
O A:HOH1337 4.2 40.4 1.0
CD1 A:LEU196 4.3 12.1 1.0
O A:LEU196 4.7 18.4 1.0
O A:HOH1268 4.7 23.6 1.0
CE A:LYS194 4.9 17.6 1.0
C A:LEU196 5.0 17.2 1.0

Bromine binding site 2 out of 15 in 1n9k

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Bromine binding site 2 out of 15 in the Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br214

b:36.4
occ:0.50
 O A:HOH1300 3.1 31.2 1.0
N A:LYS152 3.2 26.4 1.0
CA A:THR151 3.7 28.1 1.0
CB A:THR151 3.7 28.5 1.0
CA A:GLY144 3.8 30.9 1.0
O A:HOH1334 3.8 36.7 1.0
O A:HOH1288 3.8 25.4 1.0
CB A:LYS152 3.9 24.1 1.0
C A:THR151 3.9 26.2 1.0
N A:GLY144 4.0 29.6 1.0
CA A:LYS152 4.1 24.0 1.0
C A:GLY144 4.2 31.7 1.0
CG2 A:THR151 4.4 26.8 1.0
O A:GLY144 4.5 30.6 1.0
C A:ALA143 4.5 28.3 1.0
O A:ALA143 4.8 29.9 1.0
N A:ASP145 4.9 32.6 1.0
CB A:ALA143 4.9 26.1 1.0
OG1 A:THR151 4.9 27.8 1.0

Bromine binding site 3 out of 15 in 1n9k

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Bromine binding site 3 out of 15 in the Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 3 of Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br215

b:40.0
occ:0.50
 ND2 A:ASN73 3.3 31.7 1.0
O A:PHE63 3.4 36.1 1.0
N A:TYR70 3.7 29.5 1.0
C A:ASP69 3.8 32.1 1.0
CB A:ASN73 3.8 33.2 1.0
CA A:TYR70 3.8 28.5 1.0
CB A:ASP69 3.9 34.9 1.0
CB A:PHE63 3.9 33.7 1.0
O A:ASP69 3.9 30.4 1.0
C A:PHE63 4.0 35.6 1.0
CB A:SER64 4.1 35.0 1.0
CG A:ASN73 4.1 33.1 1.0
CA A:PHE63 4.5 35.1 1.0
CA A:ASP69 4.5 34.3 1.0
OG A:SER64 4.5 35.7 1.0
CB A:TYR70 4.6 28.3 1.0
N A:SER64 4.6 35.6 1.0
CA A:SER64 4.9 34.3 1.0
C A:TYR70 4.9 26.7 1.0
CG A:PHE63 4.9 31.6 1.0

Bromine binding site 4 out of 15 in 1n9k

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Bromine binding site 4 out of 15 in the Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 4 of Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br216

b:34.3
occ:0.50
 O A:HOH1269 2.9 16.2 1.0
N A:ASP169 3.1 17.8 1.0
O A:HOH1237 3.3 15.1 1.0
CG A:PRO197 3.7 15.7 1.0
CG A:ASP169 3.7 21.1 1.0
CB A:PRO197 3.7 14.4 1.0
CB A:ASP169 3.7 21.6 1.0
CA A:SER168 3.8 17.9 1.0
OD1 A:ASP169 3.9 23.2 1.0
C A:SER168 3.9 17.9 1.0
CB A:SER168 4.0 19.0 1.0
CA A:ASP169 4.0 20.2 1.0
OD2 A:ASP169 4.1 25.8 1.0
O A:HOH1239 4.2 26.6 1.0
CA A:PRO197 4.4 16.1 1.0
OG A:SER168 4.4 22.1 1.0
NH2 A:ARG187 4.6 15.0 1.0
O A:HOH1316 4.7 29.5 1.0
NH1 A:ARG184 4.7 18.9 1.0
CD A:PRO197 5.0 15.1 1.0

Bromine binding site 5 out of 15 in 1n9k

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Bromine binding site 5 out of 15 in the Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 5 of Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br217

b:58.1
occ:0.50
 N A:GLU66 3.3 43.2 1.0
CB A:GLU66 3.5 46.3 1.0
C A:SER64 3.6 35.0 1.0
CA A:SER64 3.6 34.3 1.0
N A:PRO65 3.6 35.9 1.0
CD A:PRO65 3.6 35.5 1.0
CG A:GLU66 3.7 49.9 1.0
CA A:GLU66 3.9 45.2 1.0
CB A:SER64 4.0 35.0 1.0
N A:SER67 4.2 45.1 1.0
O A:SER64 4.2 33.8 1.0
OG A:SER67 4.3 45.7 1.0
C A:GLU66 4.3 45.1 1.0
C A:PRO65 4.4 40.5 1.0
CG A:PRO65 4.4 38.6 1.0
CA A:PRO65 4.5 38.3 1.0
O A:PHE63 4.7 36.1 1.0
CB A:PRO65 4.7 38.0 1.0
N A:SER64 4.8 35.6 1.0

Bromine binding site 6 out of 15 in 1n9k

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Bromine binding site 6 out of 15 in the Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 6 of Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br218

b:61.4
occ:0.50
 ND2 A:ASN31 3.5 15.0 1.0
O A:GLN28 3.6 24.8 1.0
CB A:GLN28 3.7 24.6 1.0
CG A:GLN28 3.8 22.3 1.0
CA A:GLN28 3.8 23.2 1.0
C A:GLN28 4.1 24.4 1.0
CB A:ASN31 4.2 15.0 1.0
CG A:ASN31 4.3 15.0 1.0
O A:HOH1416 4.5 45.2 1.0
CD A:GLN28 4.8 23.0 1.0
N A:SER32 4.8 28.8 1.0

Bromine binding site 7 out of 15 in 1n9k

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Bromine binding site 7 out of 15 in the Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 7 of Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br219

b:23.1
occ:0.50
 NE2 A:GLN96 3.5 22.3 1.0
CD A:ARG95 4.0 18.6 1.0
CB A:GLU92 4.0 14.6 1.0
CG A:GLU92 4.1 19.9 1.0
O A:GLU92 4.1 15.8 1.0
CB A:ARG95 4.1 16.3 1.0
CA A:GLU92 4.2 15.0 1.0
CG A:GLN96 4.2 18.5 1.0
OE1 A:GLU92 4.3 27.7 1.0
CD A:GLU92 4.3 23.1 1.0
CD A:GLN96 4.3 22.6 1.0
C A:GLU92 4.5 15.8 1.0
CG A:ARG95 4.6 16.8 1.0
O A:HOH1280 4.9 25.1 1.0
NE A:ARG95 5.0 18.1 1.0
OE2 A:GLU92 5.0 26.5 1.0

Bromine binding site 8 out of 15 in 1n9k

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Bromine binding site 8 out of 15 in the Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 8 of Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Br220

b:27.8
occ:0.50
 NE2 B:GLN96 3.6 21.0 1.0
CB B:GLU92 3.8 18.0 1.0
CD B:ARG95 3.9 23.6 1.0
CG B:GLU92 4.0 22.7 1.0
O B:GLU92 4.1 18.4 1.0
CG B:GLN96 4.1 20.9 1.0
CB B:ARG95 4.1 19.3 1.0
CA B:GLU92 4.2 18.0 1.0
CD B:GLU92 4.4 29.8 1.0
CD B:GLN96 4.4 26.5 1.0
OE1 B:GLU92 4.4 35.6 1.0
C B:GLU92 4.5 18.4 1.0
CG B:ARG95 4.6 21.8 1.0
NE B:ARG95 5.0 21.7 1.0

Bromine binding site 9 out of 15 in 1n9k

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Bromine binding site 9 out of 15 in the Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 9 of Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Br221

b:33.8
occ:0.50
 O B:HOH1243 3.0 17.9 1.0
O B:HOH1376 3.2 33.5 1.0
N B:LEU196 3.3 18.8 1.0
CG B:LEU196 3.7 17.9 1.0
O B:HOH1326 3.7 33.3 1.0
CA B:PRO195 3.8 22.4 1.0
CB B:PRO195 3.9 23.5 1.0
CB B:LEU196 3.9 17.2 1.0
C B:PRO195 4.0 20.7 1.0
CD B:LYS194 4.1 22.1 1.0
CA B:LEU196 4.2 18.9 1.0
CD1 B:LEU196 4.2 16.6 1.0
O B:HOH1259 4.7 23.4 1.0
O B:HOH1264 4.9 33.8 1.0
CD2 B:LEU196 4.9 12.4 1.0
O B:LEU196 4.9 19.4 1.0
CE B:LYS194 5.0 24.1 1.0

Bromine binding site 10 out of 15 in 1n9k

Go back to Bromine Binding Sites List in 1n9k
Bromine binding site 10 out of 15 in the Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 10 of Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Br222

b:37.1
occ:0.50
 O B:HOH1283 2.8 36.3 1.0
N B:LYS152 3.2 28.3 1.0
CA B:THR151 3.6 30.8 1.0
CA B:GLY144 3.7 33.6 1.0
CB B:THR151 3.7 30.7 1.0
CB B:LYS152 3.9 25.1 1.0
O B:HOH1329 3.9 39.7 1.0
O B:HOH1327 3.9 27.0 1.0
C B:THR151 4.0 29.3 1.0
N B:GLY144 4.0 31.1 1.0
CA B:LYS152 4.2 26.1 1.0
C B:GLY144 4.3 35.2 1.0
C B:ALA143 4.4 30.1 1.0
CG2 B:THR151 4.5 29.8 1.0
O B:GLY144 4.5 34.8 1.0
CB B:ALA143 4.6 28.4 1.0
O B:ALA143 4.7 31.2 1.0
OD1 B:ASP145 4.8 52.5 1.0
N B:THR151 4.9 32.2 1.0
OG1 B:THR151 4.9 29.7 1.0
N B:ASP145 5.0 38.1 1.0

Reference:

V.Calderone, C.Forleo, M.Benvenuti, M.C.Thaller, G.M.Rossolini, S.Mangani. The First Structure of A Bacterial Class B Acid Phosphatase Reveals Further Structural Heterogeneity Among Phosphatases of the Haloacid Dehalogenase Fold. J.Mol.Biol. V. 335 761 2004.
ISSN: ISSN 0022-2836
PubMed: 14687572
DOI: 10.1016/J.JMB.2003.10.050
Page generated: Wed Jul 10 17:01:19 2024

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