Bromine in PDB 5dqe: Crystal Structure of Human Transcription Factor TEAD2 in Complex with Bromo-Fenamic Acid

The structure of Crystal Structure of Human Transcription Factor TEAD2 in Complex with Bromo-Fenamic Acid, PDB code: 5dqe was solved by X.Han, X.Luo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.67 / 2.18
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	121.470, 61.582, 80.419, 90.00, 117.70, 90.00
R / Rfree (%)	17.9 / 22.7

The binding sites of Bromine atom in the Crystal Structure of Human Transcription Factor TEAD2 in Complex with Bromo-Fenamic Acid (pdb code 5dqe). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 3 binding sites of Bromine where determined in the Crystal Structure of Human Transcription Factor TEAD2 in Complex with Bromo-Fenamic Acid, PDB code: 5dqe:
Jump to Bromine binding site number: 1; 2; 3;

Bromine binding site 1 out of 3 in the Crystal Structure of Human Transcription Factor TEAD2 in Complex with Bromo-Fenamic Acid


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 Human Transcription Factor TEAD2 in Complex with Bromo-Fenamic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Br501 b:0.6 occ:1.00 BR A:5E4501 0.0 0.6 1.0 CAN A:5E4501 1.9 83.1 1.0 CAM A:5E4501 2.8 38.6 1.0 HAM A:5E4501 2.8 46.3 1.0 HZ A:PHE233 2.9 39.4 1.0 CAG A:5E4501 2.9 36.0 1.0 HAG A:5E4501 3.0 43.2 1.0 CZ A:PHE233 3.4 32.8 1.0 HE2 A:PHE302 3.5 55.5 1.0 HZ A:PHE428 3.5 29.1 1.0 CD1 A:TYR426 3.5 34.4 1.0 CG A:TYR426 3.5 31.5 1.0 CD2 A:TYR426 3.6 31.1 1.0 CE1 A:TYR426 3.6 34.2 1.0 HE2 A:PHE233 3.6 42.9 1.0 HG21 A:ILE408 3.6 27.1 1.0 CZ A:TYR426 3.6 35.4 1.0 CE2 A:TYR426 3.6 31.2 1.0 CE2 A:PHE233 3.7 35.7 1.0 HD12 A:ILE408 3.8 36.6 1.0 HD1 A:TYR426 3.9 41.3 1.0 HD2 A:TYR426 4.0 37.3 1.0 HE1 A:TYR426 4.0 41.1 1.0 HB2 A:TYR426 4.1 33.3 1.0 HE2 A:TYR426 4.1 37.5 1.0 CAL A:5E4501 4.1 40.1 1.0 HD13 A:ILE408 4.2 36.6 1.0 CAF A:5E4501 4.2 41.6 1.0 CE1 A:PHE233 4.2 39.7 1.0 HB A:ILE408 4.3 27.9 1.0 CB A:TYR426 4.3 27.8 1.0 HB3 A:TYR426 4.3 33.3 1.0 HAC A:5E4501 4.3 85.4 1.0 OH A:TYR426 4.4 36.1 1.0 CE2 A:PHE302 4.4 46.3 1.0 CG2 A:ILE408 4.4 22.6 1.0 CZ A:PHE428 4.4 24.2 1.0 HG22 A:ILE408 4.4 27.1 1.0 HE1 A:PHE233 4.4 47.7 1.0 CD1 A:ILE408 4.4 30.5 1.0 HG3 A:GLN410 4.6 55.7 1.0 HH A:TYR426 4.6 43.3 1.0 CAE A:5E4501 4.6 72.8 1.0 HE2 A:PHE428 4.7 31.6 1.0 HG21 A:VAL252 4.8 57.6 1.0 CB A:ILE408 4.8 23.3 1.0 CD2 A:PHE233 4.8 33.6 1.0 HAF A:5E4501 4.9 49.9 1.0 HD2 A:PHE302 5.0 45.5 1.0

Bromine binding site 2 out of 3 in the Crystal Structure of Human Transcription Factor TEAD2 in Complex with Bromo-Fenamic Acid


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 Human Transcription Factor TEAD2 in Complex with Bromo-Fenamic Acid within 5.0Å range: probe atom residue distance (Å) B Occ B:Br501 b:0.5 occ:1.00 BR B:5E4501 0.0 0.5 1.0 CAN B:5E4501 1.9 64.0 1.0 CAM B:5E4501 2.8 41.5 1.0 HAM B:5E4501 2.9 49.8 1.0 CAG B:5E4501 2.9 29.1 1.0 HAG B:5E4501 3.0 35.0 1.0 HZ B:PHE233 3.1 38.3 1.0 HG21 B:ILE408 3.2 18.0 1.0 CD2 B:TYR426 3.5 21.5 1.0 CZ B:PHE233 3.6 31.9 1.0 HZ B:PHE428 3.6 20.5 1.0 CE2 B:TYR426 3.6 20.1 1.0 HE2 B:PHE233 3.6 35.1 1.0 CG B:TYR426 3.6 22.5 1.0 HE2 B:PHE302 3.7 22.4 1.0 CZ B:TYR426 3.8 23.0 1.0 CD1 B:TYR426 3.8 20.1 1.0 HD12 B:ILE408 3.8 20.2 1.0 HD2 B:TYR426 3.8 25.8 1.0 CE2 B:PHE233 3.9 29.2 1.0 HD13 B:ILE408 3.9 20.2 1.0 HB B:ILE408 3.9 16.2 1.0 CE1 B:TYR426 3.9 25.3 1.0 CG2 B:ILE408 3.9 15.0 1.0 HG22 B:ILE408 3.9 18.0 1.0 HE2 B:TYR426 4.0 24.2 1.0 CAL B:5E4501 4.1 37.0 1.0 HB2 B:TYR426 4.1 23.6 1.0 CAF B:5E4501 4.2 28.6 1.0 HB3 B:TYR426 4.3 23.6 1.0 HD1 B:TYR426 4.3 24.1 1.0 CD1 B:ILE408 4.3 16.8 1.0 CB B:TYR426 4.3 19.7 1.0 CB B:ILE408 4.4 13.5 1.0 HG3 B:GLN410 4.4 56.7 1.0 HE1 B:TYR426 4.4 30.3 1.0 HAC B:5E4501 4.4 85.3 1.0 CZ B:PHE428 4.5 17.1 1.0 CE1 B:PHE233 4.5 24.7 1.0 OH B:TYR426 4.6 27.3 1.0 CE2 B:PHE302 4.6 18.7 1.0 CAE B:5E4501 4.6 43.2 1.0 CD B:GLN410 4.7 42.8 1.0 NE2 B:GLN410 4.7 39.7 1.0 HG23 B:ILE408 4.7 18.0 1.0 HE1 B:PHE233 4.7 29.6 1.0 HH B:TYR426 4.8 32.7 1.0 HE22 B:GLN410 4.8 47.6 1.0 HE21 B:GLN410 4.9 47.6 1.0 OE1 B:GLN410 4.9 29.5 1.0 HAF B:5E4501 4.9 34.4 1.0 HE2 B:PHE428 4.9 20.9 1.0 HG21 B:VAL252 4.9 28.2 1.0 CG1 B:ILE408 5.0 18.6 1.0

Bromine binding site 3 out of 3 in the Crystal Structure of Human Transcription Factor TEAD2 in Complex with Bromo-Fenamic Acid


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 Human Transcription Factor TEAD2 in Complex with Bromo-Fenamic Acid within 5.0Å range: probe atom residue distance (Å) B Occ B:Br502 b:1.0 occ:1.00 BR B:5E4502 0.0 1.0 1.0 CAN B:5E4502 1.9 0.7 1.0 HD2 B:LYS277 2.7 82.4 1.0 CAG B:5E4502 2.9 77.6 1.0 HG3 B:LYS277 2.9 71.4 1.0 CAM B:5E4502 2.9 85.9 1.0 HAG B:5E4502 2.9 93.1 1.0 HAM B:5E4502 3.0 0.1 1.0 HG11 B:VAL427 3.1 23.8 1.0 CD B:LYS277 3.5 68.7 1.0 CG B:LYS277 3.5 59.5 1.0 HG22 B:ILE274 3.6 52.1 1.0 HZ2 B:LYS277 3.7 97.0 1.0 HB B:ILE274 3.8 48.6 1.0 HB2 B:LYS277 3.9 58.5 1.0 CG1 B:VAL427 3.9 19.8 1.0 HG12 B:VAL427 3.9 23.8 1.0 HB3 B:LYS277 4.1 58.5 1.0 CB B:LYS277 4.1 48.7 1.0 HZ3 B:LYS277 4.1 97.0 1.0 HD3 B:LYS277 4.1 82.4 1.0 CAF B:5E4502 4.2 57.7 1.0 CAL B:5E4502 4.2 67.5 1.0 HG21 B:ILE274 4.2 52.1 1.0 NZ B:LYS277 4.3 80.8 1.0 CG2 B:ILE274 4.3 43.4 1.0 HG21 B:THR407 4.3 31.4 1.0 HG2 B:LYS277 4.4 71.4 1.0 HE2 B:PHE278 4.4 52.9 1.0 CE B:LYS277 4.5 66.8 1.0 HB B:VAL427 4.5 25.2 1.0 CB B:ILE274 4.5 40.5 1.0 HA B:ILE274 4.5 53.4 1.0 HG13 B:VAL427 4.5 23.8 1.0 HG21 B:VAL427 4.6 22.2 1.0 HG22 B:THR407 4.7 31.4 1.0 CAE B:5E4502 4.7 37.1 1.0 CB B:VAL427 4.7 21.0 1.0 HAF B:5E4502 4.9 69.2 1.0 HE3 B:LYS277 4.9 80.1 1.0 CG2 B:THR407 5.0 26.2 1.0

A.V.Pobbati, X.Han, A.W.Hung, S.Weiguang, N.Huda, G.Y.Chen, C.Kang, C.S.Chia, X.Luo, W.Hong, A.Poulsen. Targeting the Central Pocket in Human Transcription Factor Tead As A Potential Cancer Therapeutic Strategy. Structure V. 23 2076 2015.
ISSN: ISSN 1878-4186
PubMed: 26592798
DOI: 10.1016/J.STR.2015.09.009