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Bromine in PDB 8gew: H-Fabp Crystal Soaked in A Bromo Palmitic Acid Solution

Protein crystallography data

The structure of H-Fabp Crystal Soaked in A Bromo Palmitic Acid Solution, PDB code: 8gew was solved by E.Howard, A.Cousido-Siah, A.Alvarez, Y.Espinosa, A.Podjarny, A.Mitschler, M.Carlevaro, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.47 / 0.97
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 33.736, 54.966, 70.747, 90, 90, 90
R / Rfree (%) 13.5 / 15.3

Bromine Binding Sites:

The binding sites of Bromine atom in the H-Fabp Crystal Soaked in A Bromo Palmitic Acid Solution (pdb code 8gew). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the H-Fabp Crystal Soaked in A Bromo Palmitic Acid Solution, PDB code: 8gew:

Bromine binding site 1 out of 1 in 8gew

Go back to Bromine Binding Sites List in 8gew
Bromine binding site 1 out of 1 in the H-Fabp Crystal Soaked in A Bromo Palmitic Acid Solution


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of H-Fabp Crystal Soaked in A Bromo Palmitic Acid Solution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br201

b:9.4
occ:0.44
BR A:J1W201 0.0 9.4 0.4
H22 A:OLA202 1.6 7.9 0.4
C15 A:J1W201 2.0 7.1 0.4
H152 A:OLA202 2.2 16.5 0.4
C2 A:OLA202 2.3 8.3 0.4
H161 A:OLA202 2.3 15.6 0.4
H31 A:OLA202 2.4 8.0 0.4
H162 A:OLA202 2.5 15.6 0.4
H151 A:J1W201 2.5 6.8 0.4
H42 A:OLA202 2.5 8.5 0.4
C16 A:OLA202 2.5 16.5 0.4
H151 A:OLA202 2.6 16.4 0.4
C15 A:OLA202 2.6 17.2 0.4
H051 A:J1W201 2.6 15.0 0.4
C3 A:OLA202 2.6 7.8 0.4
C17 A:J1W201 2.7 6.4 0.4
C1 A:OLA202 2.8 7.0 0.4
H031 A:J1W201 2.9 12.5 0.4
H132 A:J1W201 2.9 7.1 0.4
C4 A:OLA202 3.1 8.6 0.4
HH22 A:ARG126 3.1 7.6 0.8
H052 A:J1W201 3.1 14.9 0.4
H21 A:OLA202 3.1 7.9 0.4
HZ A:PHE16 3.2 7.3 1.0
C05 A:J1W201 3.2 15.4 0.4
O18 A:J1W201 3.2 7.1 0.4
HH11 A:ARG126 3.3 5.4 0.2
H041 A:J1W201 3.3 15.0 0.4
H122 A:OLA202 3.3 13.8 0.4
O2 A:OLA202 3.4 7.6 0.4
O1 A:OLA202 3.4 7.0 0.4
C14 A:J1W201 3.4 5.5 0.4
O19 A:J1W201 3.5 7.0 0.4
C04 A:J1W201 3.5 15.2 0.4
H32 A:OLA202 3.6 8.0 0.4
C03 A:J1W201 3.6 13.5 0.4
HG2 A:PRO38 3.6 7.8 1.0
C13 A:J1W201 3.6 7.5 0.4
H121 A:J1W201 3.7 8.1 0.4
H51 A:OLA202 3.7 9.3 0.4
H022 A:J1W201 3.8 9.4 0.4
H81 A:OLA202 3.8 10.4 0.4
NH1 A:ARG126 3.8 5.5 0.2
NH2 A:ARG126 3.8 7.9 0.8
H41 A:OLA202 3.8 8.4 0.4
CZ A:PHE16 3.9 7.5 1.0
C5 A:OLA202 3.9 9.4 0.4
C02 A:J1W201 3.9 9.0 0.4
HG21 A:THR53 3.9 7.7 1.0
H141 A:J1W201 4.0 5.9 0.4
HH12 A:ARG126 4.0 5.5 0.2
C17 A:OLA202 4.0 12.4 0.4
C14 A:OLA202 4.1 15.7 0.4
H021 A:J1W201 4.1 9.5 0.4
O A:HOH467 4.2 13.2 0.5
H091 A:J1W201 4.2 9.1 0.4
C12 A:OLA202 4.2 13.5 0.4
HH21 A:ARG126 4.2 7.6 0.8
H142 A:J1W201 4.2 5.9 0.4
C12 A:J1W201 4.2 8.3 0.4
H52 A:OLA202 4.3 9.3 0.4
H121 A:OLA202 4.3 13.8 0.4
HE2 A:PHE16 4.3 7.1 1.0
H172 A:OLA202 4.4 12.8 0.4
HH A:TYR128 4.4 20.0 0.0
HE A:ARG126 4.4 7.5 0.8
HE A:ARG126 4.5 5.7 0.2
CG A:PRO38 4.5 8.1 1.0
HG3 A:PRO38 4.5 7.9 1.0
CE2 A:PHE16 4.5 7.4 1.0
H171 A:OLA202 4.5 12.7 0.4
H141 A:OLA202 4.5 15.6 0.4
O A:HOH423 4.5 8.1 0.9
C06 A:J1W201 4.5 13.8 0.4
O A:HOH359 4.5 8.5 1.0
H142 A:OLA202 4.6 15.2 0.4
H032 A:J1W201 4.6 12.6 0.4
H042 A:J1W201 4.6 14.8 0.4
H062 A:J1W201 4.6 13.3 0.4
CZ A:ARG126 4.6 7.0 0.8
H182 A:OLA202 4.6 12.4 0.4
H102 A:J1W201 4.6 8.5 0.4
CZ A:ARG126 4.6 5.3 0.2
H131 A:J1W201 4.6 7.1 0.4
HE1 A:PHE16 4.7 7.2 1.0
CE1 A:PHE16 4.7 7.4 1.0
C13 A:OLA202 4.7 15.7 0.4
NE A:ARG126 4.8 7.5 0.8
C8 A:OLA202 4.8 10.5 0.4
CG2 A:THR53 4.8 8.1 1.0
H082 A:J1W201 4.8 9.5 0.4
C18 A:OLA202 4.8 12.5 0.4
NE A:ARG126 4.8 5.7 0.2
HG23 A:THR53 4.9 7.7 1.0
H183 A:OLA202 4.9 12.5 0.4
O A:HOH467 5.0 6.0 0.5
C09 A:J1W201 5.0 9.1 0.4

Reference:

H.A.Alvarez, A.Cousido-Siah, Y.R.Espinosa, A.Podjarny, C.M.Carlevaro, E.Howard. Lipid Exchange in Crystal-Confined Fatty Acid Binding Proteins: X-Ray Evidence and Molecular Dynamics Explanation. Proteins 2023.
ISSN: ESSN 1097-0134
PubMed: 37462340
DOI: 10.1002/PROT.26546
Page generated: Thu Jul 11 05:11:19 2024

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