Iron in PDB 2yaj: Crystal Structure of Glycyl Radical Enzyme with Bound Substrate

All present enzymatic activity of Crystal Structure of Glycyl Radical Enzyme with Bound Substrate:
4.1.1.83;

The structure of Crystal Structure of Glycyl Radical Enzyme with Bound Substrate, PDB code: 2yaj was solved by B.M.Martins, M.Blaser, M.Feliks, G.M.Ullmann, T.Selmer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.16 / 1.81
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	133.049, 228.588, 148.226, 90.00, 90.00, 90.00
R / Rfree (%)	18.8 / 24.4

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 16;

Binding sites:

The binding sites of Iron atom in the Crystal Structure of Glycyl Radical Enzyme with Bound Substrate (pdb code 2yaj). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 16 binding sites of Iron where determined in the Crystal Structure of Glycyl Radical Enzyme with Bound Substrate, PDB code: 2yaj:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 16 in the Crystal Structure of Glycyl Radical Enzyme with Bound Substrate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Glycyl Radical Enzyme with Bound Substrate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe87 b:46.9 occ:1.00 FE1 B:SF487 0.0 46.9 1.0 S2 B:SF487 2.3 43.0 1.0 S3 B:SF487 2.3 42.2 1.0 S4 B:SF487 2.3 48.1 1.0 SG B:CYS6 2.5 44.3 1.0 FE3 B:SF487 2.7 50.8 1.0 FE2 B:SF487 2.7 46.6 1.0 FE4 B:SF487 2.8 45.1 1.0 HB3 B:CYS6 3.0 36.9 1.0 HB2 B:ASN8 3.0 41.1 1.0 CB B:CYS6 3.1 30.8 1.0 HB2 B:CYS6 3.1 36.9 1.0 HA B:PHE39 3.6 58.3 1.0 HA B:HIS3 3.7 49.6 1.0 HD21 B:ASN8 3.8 44.8 1.0 CB B:ASN8 4.0 34.3 1.0 HD2 B:PHE39 4.0 63.8 1.0 S1 B:SF487 4.0 54.9 1.0 H B:ASN8 4.1 39.1 1.0 HB3 B:ASN8 4.2 41.1 1.0 H B:CYS36 4.6 71.5 1.0 H B:LYS40 4.6 66.8 1.0 CA B:PHE39 4.6 48.6 1.0 ND2 B:ASN8 4.6 37.4 1.0 CA B:CYS6 4.6 28.4 1.0 H B:TYR9 4.6 39.9 1.0 ND1 B:HIS3 4.6 33.7 1.0 CA B:HIS3 4.7 41.5 1.0 CD2 B:PHE39 4.7 53.2 1.0 HB3 B:HIS3 4.7 47.0 1.0 CA B:ASN8 4.7 34.3 1.0 HB2 B:PHE39 4.7 52.0 1.0 N B:TYR9 4.8 33.3 1.0 N B:ASN8 4.8 32.7 1.0 CG B:ASN8 4.8 32.4 1.0 HB2 B:TYR9 4.8 41.8 1.0 C B:ASN8 4.8 41.1 1.0 O B:HIS3 4.9 36.0 1.0 HD13 B:LEU21 4.9 67.2 1.0 SG B:CYS19 4.9 40.4 1.0 HA B:CYS6 5.0 34.0 1.0

Iron binding site 2 out of 16 in the Crystal Structure of Glycyl Radical Enzyme with Bound Substrate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Glycyl Radical Enzyme with Bound Substrate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe87 b:46.6 occ:1.00 FE2 B:SF487 0.0 46.6 1.0 ND1 B:HIS3 2.0 33.7 1.0 S2 B:SF487 2.2 43.0 1.0 S3 B:SF487 2.3 42.2 1.0 S1 B:SF487 2.4 54.9 1.0 FE4 B:SF487 2.7 45.1 1.0 FE3 B:SF487 2.7 50.8 1.0 FE1 B:SF487 2.7 46.9 1.0 CE1 B:HIS3 2.9 46.0 1.0 HA B:HIS3 2.9 49.6 1.0 HE1 B:HIS3 3.0 55.1 1.0 CG B:HIS3 3.0 44.7 1.0 HB3 B:HIS3 3.2 47.0 1.0 CB B:HIS3 3.4 39.2 1.0 CA B:HIS3 3.6 41.5 1.0 HB2 B:CYS19 3.7 35.0 1.0 S4 B:SF487 3.9 48.1 1.0 H B:CYS36 3.9 71.5 1.0 NE2 B:HIS3 4.0 45.0 1.0 CD2 B:HIS3 4.1 49.0 1.0 HG22 B:VAL26 4.2 31.8 1.0 HB3 B:CYS36 4.2 68.7 1.0 HA B:ALA35 4.2 0.2 1.0 HG12 B:VAL26 4.2 51.3 1.0 N B:HIS3 4.4 39.3 1.0 HB3 B:CYS6 4.4 36.9 1.0 HB2 B:HIS3 4.4 47.0 1.0 H B:HIS3 4.4 47.1 1.0 CB B:CYS19 4.6 29.2 1.0 HB2 B:CYS6 4.6 36.9 1.0 N B:CYS36 4.7 59.6 1.0 SG B:CYS19 4.7 40.4 1.0 HA B:CYS19 4.7 43.8 1.0 HE2 B:HIS3 4.8 53.9 1.0 C B:HIS3 4.8 32.4 1.0 CB B:CYS6 4.9 30.8 1.0 SG B:CYS36 4.9 50.5 1.0 CB B:CYS36 5.0 57.3 1.0 HD2 B:HIS3 5.0 58.8 1.0 O B:HIS3 5.0 36.0 1.0

Iron binding site 3 out of 16 in the Crystal Structure of Glycyl Radical Enzyme with Bound Substrate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of Glycyl Radical Enzyme with Bound Substrate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe87 b:50.8 occ:1.00 FE3 B:SF487 0.0 50.8 1.0 S4 B:SF487 2.3 48.1 1.0 S1 B:SF487 2.3 54.9 1.0 S2 B:SF487 2.4 43.0 1.0 SG B:CYS36 2.5 50.5 1.0 FE1 B:SF487 2.7 46.9 1.0 FE4 B:SF487 2.7 45.1 1.0 FE2 B:SF487 2.7 46.6 1.0 HB3 B:CYS36 3.0 68.7 1.0 H B:CYS36 3.1 71.5 1.0 CB B:CYS36 3.3 57.3 1.0 HB2 B:ASN38 3.8 70.1 1.0 N B:CYS36 3.8 59.6 1.0 S3 B:SF487 3.9 42.2 1.0 CA B:CYS36 4.1 56.8 1.0 HB2 B:CYS36 4.1 68.7 1.0 HA B:PHE39 4.2 58.3 1.0 O B:CYS36 4.3 79.8 1.0 H B:ASN38 4.4 79.6 1.0 HD13 B:LEU21 4.4 67.2 1.0 HE1 B:HIS3 4.4 55.1 1.0 ND1 B:HIS3 4.4 33.7 1.0 C B:CYS36 4.5 69.4 1.0 N B:PHE39 4.5 44.3 1.0 CB B:ASN38 4.6 58.5 1.0 HB3 B:ASN38 4.6 70.1 1.0 H B:PHE39 4.6 53.0 1.0 HB2 B:PHE39 4.6 52.0 1.0 C B:ASN38 4.7 53.7 1.0 HD21 B:ASN8 4.7 44.8 1.0 SG B:CYS19 4.8 40.4 1.0 HA B:ALA35 4.8 0.2 1.0 CE1 B:HIS3 4.8 46.0 1.0 CA B:PHE39 4.8 48.6 1.0 SG B:CYS6 4.9 44.3 1.0 HA B:CYS36 5.0 68.1 1.0 N B:ASN38 5.0 66.4 1.0 HB2 B:ASN8 5.0 41.1 1.0 HD2 B:PHE39 5.0 63.8 1.0 HB2 B:CYS19 5.0 35.0 1.0

Iron binding site 4 out of 16 in the Crystal Structure of Glycyl Radical Enzyme with Bound Substrate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of Glycyl Radical Enzyme with Bound Substrate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe87 b:45.1 occ:1.00 FE4 B:SF487 0.0 45.1 1.0 S4 B:SF487 2.2 48.1 1.0 SG B:CYS19 2.3 40.4 1.0 S3 B:SF487 2.3 42.2 1.0 S1 B:SF487 2.4 54.9 1.0 FE3 B:SF487 2.7 50.8 1.0 HB2 B:CYS19 2.7 35.0 1.0 FE2 B:SF487 2.7 46.6 1.0 FE1 B:SF487 2.8 46.9 1.0 CB B:CYS19 3.0 29.2 1.0 HA B:CYS19 3.5 43.8 1.0 CA B:CYS19 3.8 36.6 1.0 HB3 B:CYS19 3.8 35.0 1.0 HB2 B:LEU21 3.9 62.2 1.0 S2 B:SF487 3.9 43.0 1.0 HB2 B:ASN8 4.0 41.1 1.0 H B:LEU21 4.0 57.4 1.0 HD13 B:LEU21 4.2 67.2 1.0 HB3 B:ASN8 4.2 41.1 1.0 HG21 B:THR22 4.3 46.0 1.0 ND1 B:HIS3 4.3 33.7 1.0 H B:ALA20 4.4 47.2 1.0 C B:CYS19 4.5 39.2 1.0 H B:THR22 4.5 44.3 1.0 CB B:ASN8 4.5 34.3 1.0 HD21 B:ASN8 4.6 44.8 1.0 HG B:LEU21 4.6 60.3 1.0 N B:ALA20 4.7 39.4 1.0 CB B:LEU21 4.8 51.9 1.0 N B:LEU21 4.8 47.9 1.0 HE1 B:HIS3 4.8 55.1 1.0 SG B:CYS36 4.8 50.5 1.0 HG12 B:VAL26 4.8 51.3 1.0 CE1 B:HIS3 5.0 46.0 1.0 CD1 B:LEU21 5.0 56.1 1.0

Iron binding site 5 out of 16 in the Crystal Structure of Glycyl Radical Enzyme with Bound Substrate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Crystal Structure of Glycyl Radical Enzyme with Bound Substrate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe88 b:33.4 occ:1.00 FE1 B:SF488 0.0 33.4 1.0 S2 B:SF488 2.3 28.8 1.0 S3 B:SF488 2.3 29.9 1.0 SG B:CYS62 2.3 27.9 1.0 S4 B:SF488 2.4 33.4 1.0 FE3 B:SF488 2.7 31.2 1.0 FE4 B:SF488 2.7 34.0 1.0 FE2 B:SF488 2.8 33.0 1.0 HB2 B:CYS62 3.0 41.8 1.0 CB B:CYS62 3.3 34.9 1.0 HH12 A:ARG61 3.3 25.7 1.0 HB2 B:ASN50 3.8 51.8 1.0 S1 B:SF488 3.8 30.8 1.0 H B:GLY64 3.8 58.9 1.0 HA B:CYS62 3.9 41.6 1.0 HA3 B:GLY64 4.0 68.3 1.0 HB3 B:CYS62 4.0 41.8 1.0 HH22 A:ARG61 4.1 25.6 1.0 NH1 A:ARG61 4.2 21.5 1.0 CA B:CYS62 4.2 34.8 1.0 HB3 B:ASN50 4.2 51.8 1.0 HD21 B:ASN50 4.3 40.4 1.0 CB B:ASN50 4.4 43.3 1.0 HB3 B:ALA71 4.5 41.8 1.0 N B:GLY64 4.6 49.1 1.0 HH11 A:ARG61 4.7 25.7 1.0 H B:THR63 4.7 38.9 1.0 SG B:CYS45 4.7 29.1 1.0 HH2 A:TRP58 4.7 30.8 1.0 CA B:GLY64 4.7 57.0 1.0 HB2 B:SER82 4.8 49.8 1.0 HB2 B:PHE51 4.8 32.4 1.0 SG B:CYS80 4.8 33.2 1.0 NH2 A:ARG61 4.8 21.4 1.0 SG B:CYS48 4.8 35.3 1.0 HB2 B:ALA71 4.9 41.8 1.0 HB3 B:CYS45 4.9 28.7 1.0 C B:CYS62 4.9 40.7 1.0 CZ A:ARG61 5.0 23.6 1.0 N B:THR63 5.0 32.5 1.0

Iron binding site 6 out of 16 in the Crystal Structure of Glycyl Radical Enzyme with Bound Substrate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Crystal Structure of Glycyl Radical Enzyme with Bound Substrate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe88 b:33.0 occ:1.00 FE2 B:SF488 0.0 33.0 1.0 S1 B:SF488 2.3 30.8 1.0 SG B:CYS80 2.3 33.2 1.0 S3 B:SF488 2.3 29.9 1.0 S4 B:SF488 2.4 33.4 1.0 FE4 B:SF488 2.7 34.0 1.0 FE3 B:SF488 2.7 31.2 1.0 FE1 B:SF488 2.8 33.4 1.0 HB3 B:CYS80 3.3 33.0 1.0 CB B:CYS80 3.3 27.5 1.0 HB2 B:CYS80 3.5 33.0 1.0 HB2 B:SER82 3.7 49.8 1.0 HH2 A:TRP58 3.8 30.8 1.0 HA B:TYR83 3.8 42.2 1.0 S2 B:SF488 3.9 28.8 1.0 H B:TYR83 4.0 44.1 1.0 HB2 B:TYR83 4.0 37.0 1.0 N B:TYR83 4.1 36.8 1.0 H B:SER82 4.1 49.9 1.0 HZ2 A:TRP58 4.3 36.9 1.0 CA B:TYR83 4.3 35.2 1.0 HD21 B:ASN50 4.5 40.4 1.0 C B:SER82 4.5 37.5 1.0 CB B:SER82 4.6 41.6 1.0 CH2 A:TRP58 4.6 25.7 1.0 HD1 B:TYR83 4.6 46.5 1.0 CB B:TYR83 4.6 30.9 1.0 HH12 A:ARG61 4.7 25.7 1.0 CA B:CYS80 4.7 26.2 1.0 SG B:CYS45 4.7 29.1 1.0 HB2 B:ALA77 4.7 32.8 1.0 SG B:CYS62 4.7 27.9 1.0 O A:HOH2035 4.8 42.2 1.0 CZ2 A:TRP58 4.8 30.8 1.0 N B:SER82 4.8 41.6 1.0 SG B:CYS48 4.8 35.3 1.0 CA B:SER82 4.9 30.2 1.0 HB3 B:SER82 5.0 49.8 1.0

Iron binding site 7 out of 16 in the Crystal Structure of Glycyl Radical Enzyme with Bound Substrate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Crystal Structure of Glycyl Radical Enzyme with Bound Substrate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe88 b:31.2 occ:1.00 FE3 B:SF488 0.0 31.2 1.0 SG B:CYS45 2.2 29.1 1.0 S2 B:SF488 2.3 28.8 1.0 S1 B:SF488 2.3 30.8 1.0 S4 B:SF488 2.4 33.4 1.0 FE1 B:SF488 2.7 33.4 1.0 FE2 B:SF488 2.7 33.0 1.0 FE4 B:SF488 2.8 34.0 1.0 HB3 B:CYS45 3.1 28.7 1.0 HA B:CYS45 3.2 30.6 1.0 CB B:CYS45 3.2 24.0 1.0 CA B:CYS45 3.7 25.6 1.0 S3 B:SF488 3.9 29.9 1.0 HB2 B:CYS45 4.1 28.7 1.0 HB2 B:ALA71 4.1 41.8 1.0 HB2 B:CYS48 4.4 40.7 1.0 HB3 B:ALA77 4.4 32.8 1.0 HB3 B:CYS48 4.4 40.7 1.0 HB2 B:PHE51 4.4 32.4 1.0 HZ2 A:TRP58 4.5 36.9 1.0 HB2 B:CYS62 4.5 41.8 1.0 N B:CYS45 4.5 30.8 1.0 HB2 B:ALA77 4.6 32.8 1.0 HH12 A:ARG61 4.6 25.7 1.0 H B:CYS45 4.6 36.9 1.0 HD1 B:TYR83 4.6 46.5 1.0 HB3 B:ALA71 4.7 41.8 1.0 CB B:CYS48 4.7 34.0 1.0 SG B:CYS80 4.7 33.2 1.0 SG B:CYS48 4.7 35.3 1.0 HH2 A:TRP58 4.8 30.8 1.0 CB B:ALA71 4.8 34.9 1.0 HD1 B:PHE51 4.8 36.5 1.0 HB2 B:CYS80 4.8 33.0 1.0 SG B:CYS62 4.8 27.9 1.0 HB3 B:CYS80 4.9 33.0 1.0 C B:CYS45 4.9 36.6 1.0 CB B:ALA77 4.9 27.4 1.0 HB3 B:CYS75 4.9 34.6 1.0 O B:HOH2053 4.9 30.1 1.0 HB1 B:ALA71 5.0 41.8 1.0

Iron binding site 8 out of 16 in the Crystal Structure of Glycyl Radical Enzyme with Bound Substrate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Crystal Structure of Glycyl Radical Enzyme with Bound Substrate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe88 b:34.0 occ:1.00 FE4 B:SF488 0.0 34.0 1.0 S1 B:SF488 2.3 30.8 1.0 S3 B:SF488 2.3 29.9 1.0 SG B:CYS48 2.3 35.3 1.0 S2 B:SF488 2.4 28.8 1.0 FE2 B:SF488 2.7 33.0 1.0 FE1 B:SF488 2.7 33.4 1.0 FE3 B:SF488 2.8 31.2 1.0 HB2 B:ASN50 3.0 51.8 1.0 HA B:TYR83 3.1 42.2 1.0 CB B:CYS48 3.2 34.0 1.0 HB2 B:CYS48 3.2 40.7 1.0 HB3 B:CYS48 3.2 40.7 1.0 HD21 B:ASN50 3.2 40.4 1.0 HD1 B:TYR83 3.7 46.5 1.0 CB B:ASN50 3.9 43.3 1.0 HA B:CYS45 3.9 30.6 1.0 S4 B:SF488 4.0 33.4 1.0 CA B:TYR83 4.0 35.2 1.0 ND2 B:ASN50 4.1 33.7 1.0 H B:ASN50 4.1 49.1 1.0 H B:LYS84 4.2 47.6 1.0 HB2 B:PHE51 4.3 32.4 1.0 HB2 B:TYR83 4.3 37.0 1.0 HB3 B:ASN50 4.3 51.8 1.0 CD1 B:TYR83 4.4 38.8 1.0 N B:TYR83 4.5 36.8 1.0 CG B:ASN50 4.6 44.4 1.0 CA B:CYS48 4.6 38.6 1.0 CB B:TYR83 4.7 30.9 1.0 H B:PHE51 4.7 40.3 1.0 SG B:CYS62 4.7 27.9 1.0 O B:SER82 4.8 35.8 1.0 SG B:CYS45 4.8 29.1 1.0 HB3 B:CYS45 4.8 28.7 1.0 SG B:CYS80 4.8 33.2 1.0 HB2 B:SER82 4.8 49.8 1.0 N B:ASN50 4.8 41.0 1.0 HB2 B:ALA77 4.8 32.8 1.0 C B:SER82 4.8 37.5 1.0 CA B:ASN50 4.8 35.8 1.0 N B:PHE51 4.8 33.7 1.0 H B:TYR83 4.8 44.1 1.0 CA B:CYS45 4.9 25.6 1.0 N B:LYS84 4.9 39.8 1.0 HD22 B:ASN50 4.9 40.4 1.0 HA B:CYS48 4.9 46.2 1.0 C B:ASN50 5.0 39.9 1.0

Iron binding site 9 out of 16 in the Crystal Structure of Glycyl Radical Enzyme with Bound Substrate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Crystal Structure of Glycyl Radical Enzyme with Bound Substrate within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe87 b:43.9 occ:1.00 FE1 D:SF487 0.0 43.9 1.0 S3 D:SF487 2.2 41.1 1.0 S2 D:SF487 2.3 38.1 1.0 SG D:CYS6 2.3 34.6 1.0 S4 D:SF487 2.5 46.7 1.0 FE4 D:SF487 2.7 42.8 1.0 FE3 D:SF487 2.7 49.7 1.0 FE2 D:SF487 2.8 50.5 1.0 HB3 D:CYS6 2.9 33.8 1.0 CB D:CYS6 3.0 28.3 1.0 HB2 D:CYS6 3.1 33.8 1.0 HB2 D:ASN8 3.1 52.8 1.0 HA D:PHE39 3.5 71.2 1.0 HD21 D:ASN8 3.5 52.9 1.0 HA D:HIS3 3.8 58.5 1.0 HD1 D:PHE39 3.8 68.0 1.0 H D:ASN8 4.0 52.0 1.0 S1 D:SF487 4.0 53.8 1.0 CB D:ASN8 4.1 44.1 1.0 H D:LYS40 4.4 63.8 1.0 ND2 D:ASN8 4.4 44.1 1.0 CA D:PHE39 4.4 59.4 1.0 HB3 D:ASN8 4.5 52.8 1.0 CA D:CYS6 4.5 31.2 1.0 ND1 D:HIS3 4.6 51.5 1.0 H D:CYS36 4.6 89.5 1.0 CD1 D:PHE39 4.6 56.7 1.0 HB2 D:PHE39 4.7 74.0 1.0 N D:ASN8 4.7 43.4 1.0 CA D:HIS3 4.7 48.8 1.0 HB3 D:HIS3 4.7 61.8 1.0 CG D:ASN8 4.8 45.5 1.0 CA D:ASN8 4.8 43.1 1.0 H D:TYR9 4.8 46.1 1.0 N D:PHE39 4.8 57.7 1.0 O D:HIS3 4.8 53.6 1.0 SG D:CYS19 4.8 46.6 1.0 HD13 D:LEU21 4.9 71.0 1.0 HA D:CYS6 4.9 37.4 1.0 C D:ASN8 4.9 38.4 1.0 SG D:CYS36 4.9 58.3 1.0 N D:TYR9 4.9 38.5 1.0 C D:CYS6 5.0 43.6 1.0

Iron binding site 10 out of 16 in the Crystal Structure of Glycyl Radical Enzyme with Bound Substrate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Crystal Structure of Glycyl Radical Enzyme with Bound Substrate within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe87 b:50.5 occ:1.00 FE2 D:SF487 0.0 50.5 1.0 ND1 D:HIS3 1.8 51.5 1.0 S1 D:SF487 2.2 53.8 1.0 S4 D:SF487 2.3 46.7 1.0 S3 D:SF487 2.5 41.1 1.0 FE3 D:SF487 2.7 49.7 1.0 FE4 D:SF487 2.7 42.8 1.0 CE1 D:HIS3 2.7 49.7 1.0 HE1 D:HIS3 2.8 59.5 1.0 FE1 D:SF487 2.8 43.9 1.0 CG D:HIS3 3.0 58.8 1.0 HA D:HIS3 3.0 58.5 1.0 HB3 D:HIS3 3.3 61.8 1.0 CB D:HIS3 3.5 51.6 1.0 CA D:HIS3 3.7 48.8 1.0 HA D:ALA35 3.7 69.4 1.0 NE2 D:HIS3 3.9 53.6 1.0 HB2 D:CYS19 3.9 44.7 1.0 CD2 D:HIS3 4.0 58.6 1.0 S2 D:SF487 4.0 38.1 1.0 H D:CYS36 4.0 89.5 1.0 HB3 D:CYS6 4.4 33.8 1.0 HB3 D:CYS36 4.4 86.2 1.0 HB2 D:HIS3 4.4 61.8 1.0 N D:HIS3 4.4 43.1 1.0 HB2 D:CYS6 4.5 33.8 1.0 H D:HIS3 4.5 51.7 1.0 HG22 D:VAL26 4.5 54.8 1.0 N D:CYS36 4.6 74.6 1.0 CA D:ALA35 4.6 57.9 1.0 HE2 D:HIS3 4.6 64.2 1.0 HG12 D:VAL26 4.7 58.2 1.0 CB D:CYS19 4.7 37.3 1.0 SG D:CYS19 4.8 46.6 1.0 CB D:CYS6 4.8 28.3 1.0 SG D:CYS36 4.8 58.3 1.0 C D:HIS3 4.9 43.3 1.0 HD2 D:HIS3 4.9 70.2 1.0 HB2 D:ALA35 4.9 66.4 1.0 SG D:CYS6 5.0 34.6 1.0 O D:GLU34 5.0 64.2 1.0 HD1 D:PHE39 5.0 68.0 1.0

B.M.Martins, M.Blaser, M.Feliks, G.M.Ullmann, W.Buckel, T.Selmer. Structural Basis For A Kolbe-Type Decarboxylation Catalyzed By A Glycyl Radical Enzyme. J.Am.Chem.Soc. V. 133 14666 2011.
ISSN: ISSN 0002-7863
PubMed: 21823587
DOI: 10.1021/JA203344X