Bromine in PDB 8fhj: Crystal Structure of A Fad Monooxygenease From Methylocystis Sp. Strain SB2

The structure of Crystal Structure of A Fad Monooxygenease From Methylocystis Sp. Strain SB2, PDB code: 8fhj was solved by A.M.Stewart, M.R.Sawaya, C.E.Stewart, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	59.95 / 2.61
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	148.347, 96.765, 135.206, 90, 116.41, 90
R / Rfree (%)	20.4 / 25.4

The structure of Crystal Structure of A Fad Monooxygenease From Methylocystis Sp. Strain SB2 also contains other interesting chemical elements:

Sodium

(Na)

1 atom

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 13;

Binding sites:

The binding sites of Bromine atom in the Crystal Structure of A Fad Monooxygenease From Methylocystis Sp. Strain SB2 (pdb code 8fhj). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 13 binding sites of Bromine where determined in the Crystal Structure of A Fad Monooxygenease From Methylocystis Sp. Strain SB2, PDB code: 8fhj:
Jump to Bromine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Bromine binding site 1 out of 13 in the Crystal Structure of A Fad Monooxygenease From Methylocystis Sp. Strain SB2


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 A Fad Monooxygenease From Methylocystis Sp. Strain SB2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br604 b:61.9 occ:0.50 NE A:ARG51 3.4 84.0 1.0 N A:ARG51 3.5 60.6 1.0 CB A:ASN50 3.6 60.7 1.0 CB A:ARG51 3.8 65.0 1.0 CG A:ARG51 3.9 71.6 1.0 CD1 A:ILE110 4.1 78.0 1.0 NH2 A:ARG51 4.1 91.3 1.0 CD1 A:LEU384 4.2 68.3 1.0 CD A:ARG51 4.2 78.6 1.0 CZ A:ARG51 4.2 90.1 1.0 CG A:ASN50 4.2 60.9 1.0 CA A:ARG51 4.2 61.2 1.0 CB A:ALA387 4.3 59.0 1.0 CA A:ASN50 4.3 61.3 1.0 C A:ASN50 4.4 61.3 1.0 ND2 A:ASN50 4.6 60.2 1.0 N A:ARG52 4.7 59.9 1.0 SD A:MET388 4.7 74.3 1.0 OD1 A:ASN50 4.8 61.1 1.0 C A:ARG51 5.0 59.5 1.0

Bromine binding site 2 out of 13 in the Crystal Structure of A Fad Monooxygenease From Methylocystis Sp. Strain SB2


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 A Fad Monooxygenease From Methylocystis Sp. Strain SB2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br605 b:77.8 occ:0.50 OG1 A:THR178 3.8 62.4 1.0 O A:GLU140 4.0 64.7 1.0 CG1 A:ILE179 4.4 58.8 1.0 N A:ILE179 4.4 57.8 1.0 C A:THR178 4.5 59.4 1.0 O A:THR178 4.5 60.9 1.0 CA A:ILE179 4.5 58.2 1.0 O A:LEU139 4.6 62.3 1.0 CE1 A:PHE142 4.6 64.6 1.0 C A:GLU140 4.6 64.3 1.0 CB A:THR178 4.7 61.1 1.0 CD1 A:PHE142 4.7 64.8 1.0 CG2 A:VAL182 4.7 62.1 1.0 CA A:ARG141 4.8 63.0 1.0 CD2 A:LEU139 4.9 61.5 1.0 N A:ARG141 4.9 61.7 1.0

Bromine binding site 3 out of 13 in the Crystal Structure of A Fad Monooxygenease From Methylocystis Sp. Strain SB2


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 A Fad Monooxygenease From Methylocystis Sp. Strain SB2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br606 b:83.4 occ:0.50 NH1 A:ARG442 3.7 88.4 1.0 CG A:ARG442 3.8 73.6 1.0 OD1 A:ASP443 3.9 74.3 1.0 CA A:ARG27 4.2 60.8 1.0 NZ A:LYS333 4.2 72.7 1.0 CB A:ARG27 4.4 60.0 1.0 NH1 A:ARG27 4.4 68.1 1.0 O A:ARG27 4.5 63.6 1.0 O A:ARG442 4.5 62.4 1.0 CG A:ARG27 4.5 61.8 1.0 C A:ARG27 4.6 62.8 1.0 CD A:ARG442 4.7 80.5 1.0 C A:ARG442 4.7 63.6 1.0 CZ A:ARG442 4.8 88.9 1.0 CA A:ARG442 4.9 63.9 1.0 CB A:ARG442 4.9 67.6 1.0 CG A:ASP443 5.0 74.5 1.0

Bromine binding site 4 out of 13 in the Crystal Structure of A Fad Monooxygenease From Methylocystis Sp. Strain SB2


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 A Fad Monooxygenease From Methylocystis Sp. Strain SB2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br607 b:93.3 occ:0.50 CD A:PRO450 3.2 81.7 1.0 CG A:PRO450 3.7 85.0 1.0 CB A:LEU475 3.8 80.9 1.0 CG A:LEU475 4.2 79.8 1.0 CB A:LEU487 4.3 82.3 1.0 N A:PRO450 4.5 81.6 1.0 CD A:PRO488 4.5 83.6 1.0 CA A:GLY449 4.6 79.9 1.0 CD2 A:LEU487 4.6 84.0 1.0 CG A:PRO488 4.9 87.0 1.0

Bromine binding site 5 out of 13 in the Crystal Structure of A Fad Monooxygenease From Methylocystis Sp. Strain SB2


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 A Fad Monooxygenease From Methylocystis Sp. Strain SB2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br608 b:70.4 occ:0.50 N A:GLY313 3.1 62.6 1.0 O A:HOH712 3.3 60.5 1.0 C10 A:FAD601 3.3 72.6 1.0 N10 A:FAD601 3.4 71.1 1.0 N A:LEU312 3.4 66.6 1.0 N1 A:FAD601 3.4 73.0 1.0 CA A:PRO308 3.5 67.2 1.0 CA A:GLY311 3.6 71.7 1.0 C1' A:FAD601 3.6 69.0 1.0 CA A:GLY313 3.8 61.0 1.0 C A:GLY311 3.8 70.2 1.0 N A:GLY311 3.9 72.8 1.0 C4X A:FAD601 4.0 73.5 1.0 O A:PRO307 4.1 64.6 1.0 CB A:PRO308 4.1 67.4 1.0 C9A A:FAD601 4.1 71.7 1.0 C2 A:FAD601 4.1 73.9 1.0 OG1 A:THR306 4.1 66.2 1.0 C A:LEU312 4.2 61.8 1.0 C A:PRO308 4.3 69.3 1.0 CA A:LEU312 4.3 64.5 1.0 N A:PRO308 4.4 66.9 1.0 C A:PRO307 4.5 64.2 1.0 N5 A:FAD601 4.6 73.4 1.0 C5X A:FAD601 4.6 72.6 1.0 N A:GLY314 4.6 59.8 1.0 C4 A:FAD601 4.6 74.7 1.0 N3 A:FAD601 4.6 74.7 1.0 N A:VAL309 4.7 66.5 1.0 O2 A:FAD601 4.7 73.8 1.0 C A:GLY313 4.7 59.3 1.0 O A:THR306 4.8 62.5 1.0 C9 A:FAD601 4.8 71.5 1.0 O A:GLY311 4.9 70.8 1.0 C2' A:FAD601 5.0 67.3 1.0

Bromine binding site 6 out of 13 in the Crystal Structure of A Fad Monooxygenease From Methylocystis Sp. Strain SB2


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 A Fad Monooxygenease From Methylocystis Sp. Strain SB2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Br610 b:63.0 occ:0.50 O B:HOH724 3.2 67.7 1.0 O B:HOH736 3.6 63.0 1.0 CD B:PRO450 3.6 66.9 1.0 CB B:LEU475 3.9 68.3 1.0 CD B:PRO488 4.0 65.3 1.0 CB B:LEU487 4.0 62.9 1.0 CG B:LEU475 4.3 69.8 1.0 CG B:PRO450 4.3 69.6 1.0 CD1 B:LEU487 4.4 63.1 1.0 CG B:PRO488 4.5 69.0 1.0 CA B:GLY449 4.5 64.6 1.0 CG B:LEU487 4.6 62.6 1.0 N B:PRO450 4.8 65.7 1.0 CD1 B:LEU475 4.9 71.6 1.0

Bromine binding site 7 out of 13 in the Crystal Structure of A Fad Monooxygenease From Methylocystis Sp. Strain SB2


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 A Fad Monooxygenease From Methylocystis Sp. Strain SB2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Br611 b:65.2 occ:0.50 NE B:ARG51 3.4 83.0 1.0 N B:ARG51 3.4 57.8 1.0 CG B:ARG51 3.6 69.4 1.0 CB B:ARG51 3.7 61.7 1.0 CB B:ASN50 3.7 57.4 1.0 CD B:ARG51 4.0 77.2 1.0 CA B:ARG51 4.2 57.8 1.0 CD1 B:LEU384 4.2 67.0 1.0 CD1 B:ILE110 4.2 72.5 1.0 CZ B:ARG51 4.2 87.7 1.0 CG B:ASN50 4.2 57.7 1.0 NH2 B:ARG51 4.2 88.5 1.0 CA B:ASN50 4.3 57.8 1.0 C B:ASN50 4.4 57.3 1.0 ND2 B:ASN50 4.4 57.1 1.0 CB B:ALA387 4.4 59.4 1.0 SD B:MET388 4.8 72.7 1.0 N B:ARG52 4.8 58.1 1.0 OD1 B:ASN50 4.9 58.9 1.0

Bromine binding site 8 out of 13 in the Crystal Structure of A Fad Monooxygenease From Methylocystis Sp. Strain SB2


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 A Fad Monooxygenease From Methylocystis Sp. Strain SB2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Br612 b:74.5 occ:0.50 NH2 B:ARG529 3.1 54.4 1.0 CB B:LYS467 3.6 55.8 1.0 NH2 B:ARG465 3.6 69.0 1.0 NH1 B:ARG529 4.0 53.0 1.0 CZ B:ARG529 4.0 54.0 1.0 CB B:ALA468 4.1 52.8 1.0 NE B:ARG465 4.1 65.0 1.0 C B:LYS467 4.1 52.0 1.0 N B:ALA468 4.1 53.4 1.0 CG B:LYS467 4.2 61.2 1.0 CA B:ALA468 4.3 52.5 1.0 O B:LYS467 4.3 52.0 1.0 CZ B:ARG465 4.3 68.5 1.0 CA B:LYS467 4.5 52.8 1.0 CB B:ARG465 4.8 53.1 1.0 CD B:LYS467 4.8 67.6 1.0

Bromine binding site 9 out of 13 in the Crystal Structure of A Fad Monooxygenease From Methylocystis Sp. Strain SB2


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 A Fad Monooxygenease From Methylocystis Sp. Strain SB2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Br613 b:64.8 occ:0.50 N B:PHE135 3.4 59.1 1.0 O3 B:GOL604 3.8 70.7 1.0 NH2 B:ARG127 3.8 66.5 1.0 O B:VAL133 4.0 56.9 1.0 CA B:ARG134 4.1 56.0 1.0 CB B:PHE135 4.1 59.3 1.0 CD2 B:PHE135 4.1 59.8 1.0 C B:ARG134 4.3 55.2 1.0 CA B:PHE135 4.3 59.3 1.0 CG B:PHE135 4.7 58.7 1.0 O B:PHE135 4.7 62.7 1.0 C B:PHE135 4.8 61.4 1.0 C B:VAL133 4.9 55.6 1.0 N B:ARG134 4.9 54.4 1.0 CZ B:ARG127 5.0 66.8 1.0

Bromine binding site 10 out of 13 in the Crystal Structure of A Fad Monooxygenease From Methylocystis Sp. Strain SB2


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 A Fad Monooxygenease From Methylocystis Sp. Strain SB2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Br614 b:95.5 occ:0.50 N B:ASN235 3.3 93.0 1.0 CA B:PRO234 3.8 93.8 1.0 CB B:PRO234 4.0 97.4 1.0 C B:PRO234 4.1 93.9 1.0 OD1 B:ASN235 4.2 106.2 1.0 CA B:ASN235 4.3 93.9 1.0 NH1 B:ARG72 4.3 91.5 1.0 CZ B:ARG72 4.4 89.8 1.0 CB B:LEU205 4.5 94.9 1.0 N B:ASP206 4.5 91.8 1.0 NE B:ARG72 4.6 88.6 1.0 CA B:ASP206 4.7 95.0 1.0 CD B:ARG72 4.8 89.1 1.0 C B:LEU205 4.8 100.8 1.0 NH2 B:ARG72 4.9 87.4 1.0 CB B:ASP206 4.9 98.8 1.0 CG B:ASN235 4.9 105.0 1.0

A.M.Stewart, P.Dershwitz, C.E.Stewart, M.R.Sawaya, T.O.Yeates, J.D.Semrau, H.Zischka, A.A.Dispirito, T.A.Bobik. Crystal Structure of Mbnf: A Nadph-Dependent Flavin Monooxygenase From Methylocystis Strain SB2 To Be Published.