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Bromine in PDB 2o29: Spectroscopic and Structural Study of the Heterotropic Linkage Between Halide and Proton Ion Binding to Gfp Proteins: E2(Gfp)-Br Complex

Protein crystallography data

The structure of Spectroscopic and Structural Study of the Heterotropic Linkage Between Halide and Proton Ion Binding to Gfp Proteins: E2(Gfp)-Br Complex, PDB code: 2o29 was solved by G.Garau, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.15 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 51.144, 62.852, 69.172, 90.00, 90.00, 90.00
R / Rfree (%) 17.8 / 20.8

Bromine Binding Sites:

The binding sites of Bromine atom in the Spectroscopic and Structural Study of the Heterotropic Linkage Between Halide and Proton Ion Binding to Gfp Proteins: E2(Gfp)-Br Complex (pdb code 2o29). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 4 binding sites of Bromine where determined in the Spectroscopic and Structural Study of the Heterotropic Linkage Between Halide and Proton Ion Binding to Gfp Proteins: E2(Gfp)-Br Complex, PDB code: 2o29:
Jump to Bromine binding site number: 1; 2; 3; 4;

Bromine binding site 1 out of 4 in 2o29

Go back to Bromine Binding Sites List in 2o29
Bromine binding site 1 out of 4 in the Spectroscopic and Structural Study of the Heterotropic Linkage Between Halide and Proton Ion Binding to Gfp Proteins: E2(Gfp)-Br Complex


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Spectroscopic and Structural Study of the Heterotropic Linkage Between Halide and Proton Ion Binding to Gfp Proteins: E2(Gfp)-Br Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br1240

b:26.7
occ:1.00
N A:VAL1068 3.1 12.1 1.0
OH A:TYR1203 3.2 17.3 1.0
N2 A:CRO1066 3.4 14.9 1.0
C1 A:CRO1066 3.4 13.9 1.0
C A:VAL1068 3.5 13.0 1.0
O A:VAL1068 3.6 12.8 1.0
CA2 A:CRO1066 3.7 14.2 1.0
N A:GLN1069 3.7 13.6 1.0
CD1 A:LEU1042 3.8 16.3 1.0
N3 A:CRO1066 3.8 13.2 1.0
CE2 A:TYR1203 3.8 15.9 1.0
C2 A:CRO1066 3.8 11.5 1.0
CA A:GLN1069 3.9 13.8 1.0
CG A:GLN1069 3.9 14.0 1.0
CA A:VAL1068 3.9 13.0 1.0
CB1 A:CRO1066 3.9 14.0 1.0
CG2 A:VAL1068 4.0 13.6 1.0
CA1 A:CRO1066 4.0 12.5 1.0
CZ A:TYR1203 4.0 16.5 1.0
OE1 A:GLU1222 4.4 17.4 0.9
CB2 A:CRO1066 4.4 13.8 1.0
C3 A:CRO1066 4.5 15.5 1.0
CB A:GLN1069 4.5 14.2 1.0
OG1 A:CRO1066 4.5 14.7 1.0
CB A:VAL1068 4.6 12.3 1.0
CG2 A:VAL1224 4.6 16.6 1.0
O2 A:CRO1066 4.6 14.3 1.0
CA3 A:CRO1066 4.6 12.6 1.0

Bromine binding site 2 out of 4 in 2o29

Go back to Bromine Binding Sites List in 2o29
Bromine binding site 2 out of 4 in the Spectroscopic and Structural Study of the Heterotropic Linkage Between Halide and Proton Ion Binding to Gfp Proteins: E2(Gfp)-Br Complex


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Spectroscopic and Structural Study of the Heterotropic Linkage Between Halide and Proton Ion Binding to Gfp Proteins: E2(Gfp)-Br Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br1241

b:28.5
occ:1.00
N A:LEU1207 3.4 14.8 1.0
O A:HOH1434 3.5 26.7 1.0
N A:TYR1145 3.5 15.4 1.0
O A:HOH1307 3.6 25.7 1.0
CA A:ASN1144 3.7 14.7 1.0
CB A:ASN1144 3.8 14.3 1.0
CA A:ALA1206 3.9 14.4 1.0
O A:LEU1207 4.0 13.6 1.0
C A:ASN1144 4.1 15.2 1.0
C A:ALA1206 4.1 14.1 1.0
O A:TYR1145 4.2 18.5 1.0
O A:SER1205 4.3 16.3 1.0
CA A:LEU1207 4.3 13.9 1.0
CB A:LEU1207 4.3 14.1 1.0
O A:HOH1383 4.4 39.3 1.0
CG A:LEU1207 4.4 13.2 1.0
CA A:TYR1145 4.6 16.3 1.0
CB A:ALA1206 4.6 13.5 1.0
C A:LEU1207 4.7 14.4 1.0
CB A:TYR1145 4.7 15.3 1.0
O A:TYR1143 4.8 14.7 1.0
C A:TYR1145 4.8 17.2 1.0
N A:ALA1206 4.9 14.5 1.0
N A:ASN1144 5.0 14.6 1.0
C A:SER1205 5.0 16.0 1.0

Bromine binding site 3 out of 4 in 2o29

Go back to Bromine Binding Sites List in 2o29
Bromine binding site 3 out of 4 in the Spectroscopic and Structural Study of the Heterotropic Linkage Between Halide and Proton Ion Binding to Gfp Proteins: E2(Gfp)-Br Complex


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 3 of Spectroscopic and Structural Study of the Heterotropic Linkage Between Halide and Proton Ion Binding to Gfp Proteins: E2(Gfp)-Br Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br1242

b:30.8
occ:1.00
O A:HOH1271 3.1 15.3 1.0
O A:HOH1275 3.3 23.2 1.0
O A:HOH1431 3.3 24.6 1.0
N A:TRP1057 3.4 12.1 1.0
CD A:PRO1058 3.8 12.0 1.0
CA A:PRO1056 3.9 12.2 1.0
CD1 A:TYR1143 3.9 14.1 1.0
O A:HOH1448 3.9 27.7 1.0
CD1 A:TRP1057 4.0 12.6 1.0
CB A:TRP1057 4.1 11.7 1.0
C A:PRO1056 4.1 12.1 1.0
CB A:PRO1056 4.1 12.3 1.0
O A:HOH1270 4.3 16.8 1.0
CA A:TRP1057 4.3 11.4 1.0
CG A:TRP1057 4.4 11.1 1.0
CB A:TYR1143 4.6 14.8 1.0
CG A:TYR1143 4.7 13.4 1.0
CE1 A:TYR1143 4.7 13.5 1.0
CG A:PRO1058 4.7 12.9 1.0
N A:PRO1058 4.9 11.6 1.0
CA A:TYR1143 4.9 14.3 1.0
O A:LEU1141 5.0 15.0 1.0
O A:HOH1338 5.0 37.7 1.0

Bromine binding site 4 out of 4 in 2o29

Go back to Bromine Binding Sites List in 2o29
Bromine binding site 4 out of 4 in the Spectroscopic and Structural Study of the Heterotropic Linkage Between Halide and Proton Ion Binding to Gfp Proteins: E2(Gfp)-Br Complex


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 4 of Spectroscopic and Structural Study of the Heterotropic Linkage Between Halide and Proton Ion Binding to Gfp Proteins: E2(Gfp)-Br Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br1243

b:36.8
occ:0.50
C A:HIS1199 3.7 14.8 1.0
CA A:HIS1199 3.8 15.2 1.0
O A:HIS1199 3.8 14.3 1.0
N A:HIS1199 3.9 15.6 1.0
CD2 A:TYR1151 4.0 17.1 1.0
CD2 A:TYR1200 4.1 18.4 1.0
C A:ASN1198 4.2 16.1 1.0
N A:TYR1200 4.3 14.3 1.0
CE2 A:TYR1151 4.4 18.5 1.0
O A:ASN1198 4.5 15.2 1.0
CB A:ASN1198 4.6 16.5 1.0
CB A:TYR1200 4.7 15.7 1.0
CG A:TYR1200 4.9 16.7 1.0
CE2 A:TYR1200 4.9 16.6 1.0

Reference:

D.Arosio, G.Garau, F.Ricci, L.Marchetti, R.Bizzarri, F.Beltram. Spectroscopic and Structural Study of Proton and Halide Ion Cooperative Binding to Gfp. Biophys.J. V. 93 232 2007.
ISSN: ISSN 0006-3495
PubMed: 17434942
DOI: 10.1529/BIOPHYSJ.106.102319
Page generated: Mon Jul 7 04:27:55 2025

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