Bromine in PDB 4m52: Structure of Mtb Lpd Bound to SL827

All present enzymatic activity of Structure of Mtb Lpd Bound to SL827:
1.8.1.4;

The structure of Structure of Mtb Lpd Bound to SL827, PDB code: 4m52 was solved by C.D.Lima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.01 / 2.40
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	82.521, 111.953, 98.034, 90.00, 94.43, 90.00
R / Rfree (%)	16.9 / 22.2

The binding sites of Bromine atom in the Structure of Mtb Lpd Bound to SL827 (pdb code 4m52). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 4 binding sites of Bromine where determined in the Structure of Mtb Lpd Bound to SL827, PDB code: 4m52:
Jump to Bromine binding site number: 1; 2; 3; 4;

Bromine binding site 1 out of 4 in the Structure of Mtb Lpd Bound to SL827


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Structure of Mtb Lpd Bound to SL827 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br502 b:54.6 occ:1.00 BR A:M52502 0.0 54.6 1.0 C12 A:M52502 1.9 40.1 1.0 C14 A:M52502 2.9 32.6 1.0 C13 A:M52502 2.9 34.0 1.0 CE1 D:HIS443 3.6 34.6 1.0 CB A:PRO13 3.7 27.7 1.0 CD A:GLU321 3.7 39.5 1.0 OE2 A:GLU321 3.8 42.7 1.0 CG A:PRO13 3.8 30.3 1.0 OE1 A:GLU321 3.9 37.7 1.0 OH A:TYR16 3.9 35.0 1.0 ND1 D:HIS443 3.9 31.8 1.0 NE2 D:HIS443 4.0 34.4 1.0 CD1 A:LEU42 4.1 38.5 1.0 N03 A:M52502 4.1 36.5 1.0 C11 A:M52502 4.2 34.2 1.0 CG A:GLU321 4.3 33.2 1.0 CA A:PRO13 4.5 34.1 1.0 CB A:ALA317 4.5 28.8 1.0 CG D:HIS443 4.5 35.1 1.0 CE2 A:TYR16 4.6 31.1 1.0 CD2 D:HIS443 4.6 31.7 1.0 SG A:CYS41 4.6 33.4 1.0 CZ A:TYR16 4.6 31.6 1.0 C15 A:M52502 4.7 36.3 1.0

Bromine binding site 2 out of 4 in the Structure of Mtb Lpd Bound to SL827


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Structure of Mtb Lpd Bound to SL827 within 5.0Å range: probe atom residue distance (Å) B Occ B:Br502 b:55.9 occ:1.00 BR B:M52502 0.0 55.9 1.0 C12 B:M52502 1.9 45.2 1.0 C14 B:M52502 2.8 35.6 1.0 C13 B:M52502 2.9 40.3 1.0 CB B:PRO13 3.6 31.7 1.0 CE1 C:HIS443 3.7 34.8 1.0 OH B:TYR16 3.8 41.5 1.0 CG B:PRO13 3.8 36.3 1.0 OE2 B:GLU321 4.0 43.8 1.0 NE2 C:HIS443 4.0 32.1 1.0 ND1 C:HIS443 4.0 33.4 1.0 CD B:GLU321 4.0 43.9 1.0 CD1 B:LEU42 4.1 37.2 1.0 C11 B:M52502 4.1 41.0 1.0 N03 B:M52502 4.2 44.6 1.0 OE1 B:GLU321 4.3 40.5 1.0 CA B:PRO13 4.3 32.8 1.0 CE2 B:TYR16 4.4 33.7 1.0 CG B:GLU321 4.4 37.5 1.0 CB B:ALA317 4.5 33.1 1.0 CD2 C:HIS443 4.5 33.4 1.0 CG C:HIS443 4.5 36.0 1.0 SG B:CYS41 4.5 34.3 1.0 CZ B:TYR16 4.5 37.8 1.0 C15 B:M52502 4.7 38.9 1.0

Bromine binding site 3 out of 4 in the Structure of Mtb Lpd Bound to SL827


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 3 of Structure of Mtb Lpd Bound to SL827 within 5.0Å range: probe atom residue distance (Å) B Occ C:Br502 b:53.3 occ:1.00 BR C:M52502 0.0 53.3 1.0 C12 C:M52502 1.9 43.8 1.0 C14 C:M52502 2.9 34.9 1.0 C13 C:M52502 2.9 40.7 1.0 CB C:PRO13 3.6 29.7 1.0 CE1 B:HIS443 3.7 39.0 1.0 CG C:PRO13 3.7 35.7 1.0 OE2 C:GLU321 3.8 41.6 1.0 CD C:GLU321 3.8 44.7 1.0 NE2 B:HIS443 4.0 32.3 1.0 ND1 B:HIS443 4.0 35.3 1.0 OH C:TYR16 4.0 37.2 1.0 OE1 C:GLU321 4.1 44.5 1.0 N03 C:M52502 4.1 42.0 1.0 C11 C:M52502 4.1 37.4 1.0 CD1 C:LEU42 4.2 35.0 1.0 CG C:GLU321 4.3 40.1 1.0 CA C:PRO13 4.3 33.8 1.0 CB C:ALA317 4.4 30.9 1.0 CD2 B:HIS443 4.4 36.7 1.0 CG B:HIS443 4.4 37.8 1.0 SG C:CYS41 4.4 32.2 1.0 CE2 C:TYR16 4.5 27.1 1.0 C15 C:M52502 4.6 34.5 1.0 CZ C:TYR16 4.7 29.9 1.0 CD C:PRO13 5.0 27.8 1.0

Bromine binding site 4 out of 4 in the Structure of Mtb Lpd Bound to SL827


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 4 of Structure of Mtb Lpd Bound to SL827 within 5.0Å range: probe atom residue distance (Å) B Occ D:Br502 b:62.3 occ:1.00 BR D:M52502 0.0 62.3 1.0 C12 D:M52502 1.9 49.3 1.0 C14 D:M52502 2.9 39.3 1.0 C13 D:M52502 2.9 45.0 1.0 CE1 A:HIS443 3.6 36.1 1.0 CB D:PRO13 3.6 33.4 1.0 CG D:PRO13 3.7 32.6 1.0 CD D:GLU321 3.8 49.5 1.0 ND1 A:HIS443 3.8 38.4 1.0 OE1 D:GLU321 3.8 49.3 1.0 NE2 A:HIS443 3.9 35.2 1.0 OE2 D:GLU321 4.0 50.7 1.0 OH D:TYR16 4.1 40.8 1.0 N03 D:M52502 4.1 46.2 1.0 C11 D:M52502 4.2 37.7 1.0 CD1 D:LEU42 4.2 34.0 1.0 CG D:GLU321 4.2 38.5 1.0 CB D:ALA317 4.3 31.7 1.0 CG A:HIS443 4.3 38.8 1.0 CA D:PRO13 4.4 33.2 1.0 CD2 A:HIS443 4.4 39.0 1.0 CE2 D:TYR16 4.5 34.3 1.0 SG D:CYS41 4.6 37.8 1.0 C15 D:M52502 4.7 40.7 1.0 CZ D:TYR16 4.8 37.6 1.0

R.Bryk, N.Arango, C.Maksymiuk, A.Balakrishnan, Y.T.Wu, C.H.Wong, T.Masquelin, P.Hipskind, C.D.Lima, C.Nathan. Lipoamide Channel-Binding Sulfonamides Selectively Inhibit Mycobacterial Lipoamide Dehydrogenase. Biochemistry V. 52 9375 2013.
ISSN: ISSN 0006-2960
PubMed: 24251446
DOI: 10.1021/BI401077F