Iron in PDB 6htk: X-Ray Structure of the Tryptophan Lyase Nosl in Complex with (R)-(+)- Indoline-2-Carboxylate

The structure of X-Ray Structure of the Tryptophan Lyase Nosl in Complex with (R)-(+)- Indoline-2-Carboxylate, PDB code: 6htk was solved by P.Amara, J.M.Mouesca, M.Bella, L.Martin, C.Saragaglia, S.Gambarelli, Y.Nicolet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.11 / 2.00
Space group	P 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	94.650, 47.010, 114.080, 90.00, 108.91, 90.00
R / Rfree (%)	16.9 / 19.7

The structure of X-Ray Structure of the Tryptophan Lyase Nosl in Complex with (R)-(+)- Indoline-2-Carboxylate also contains other interesting chemical elements:

Potassium	(K)	1 atom
Bromine	(Br)	6 atoms
Sodium	(Na)	2 atoms

The binding sites of Iron atom in the X-Ray Structure of the Tryptophan Lyase Nosl in Complex with (R)-(+)- Indoline-2-Carboxylate (pdb code 6htk). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 8 binding sites of Iron where determined in the X-Ray Structure of the Tryptophan Lyase Nosl in Complex with (R)-(+)- Indoline-2-Carboxylate, PDB code: 6htk:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Iron binding site 1 out of 8 in the X-Ray Structure of the Tryptophan Lyase Nosl in Complex with (R)-(+)- Indoline-2-Carboxylate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of X-Ray Structure of the Tryptophan Lyase Nosl in Complex with (R)-(+)- Indoline-2-Carboxylate within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:35.7 occ:1.00 FE1 A:SF4501 0.0 35.7 1.0 S3 A:SF4501 2.3 36.5 1.0 S2 A:SF4501 2.3 36.7 1.0 S4 A:SF4501 2.3 36.0 1.0 SG A:CYS95 2.3 33.5 1.0 FE3 A:SF4501 2.7 36.2 1.0 FE2 A:SF4501 2.7 36.0 1.0 FE4 A:SF4501 2.8 35.6 1.0 CB A:CYS95 3.4 33.2 1.0 S1 A:SF4501 3.9 38.2 1.0 N A:MET509 4.0 86.1 0.8 N A:SAH508 4.1 15.8 0.4 CB A:SER97 4.1 42.6 1.0 N A:GLU143 4.3 33.7 1.0 CA A:GLY142 4.5 30.6 1.0 O A:MET509 4.6 0.0 0.8 O A:MET104 4.7 38.9 1.0 O A:SAH508 4.7 16.5 0.4 SG A:CYS102 4.7 34.6 1.0 N A:SER97 4.7 36.7 1.0 CB A:MET104 4.8 32.5 1.0 CA A:SER97 4.8 43.8 1.0 SG A:CYS99 4.8 38.9 1.0 CA A:CYS95 4.8 33.5 1.0 C A:MET104 4.8 37.6 1.0 C A:SER97 4.8 48.1 1.0 O A:SER97 4.9 38.2 1.0 C A:GLY142 4.9 31.7 1.0

Iron binding site 2 out of 8 in the X-Ray Structure of the Tryptophan Lyase Nosl in Complex with (R)-(+)- Indoline-2-Carboxylate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of X-Ray Structure of the Tryptophan Lyase Nosl in Complex with (R)-(+)- Indoline-2-Carboxylate within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:36.0 occ:1.00 FE2 A:SF4501 0.0 36.0 1.0 SG A:CYS99 2.3 38.9 1.0 S3 A:SF4501 2.3 36.5 1.0 S4 A:SF4501 2.3 36.0 1.0 S1 A:SF4501 2.3 38.2 1.0 FE3 A:SF4501 2.7 36.2 1.0 FE1 A:SF4501 2.7 35.7 1.0 FE4 A:SF4501 2.7 35.6 1.0 CB A:CYS99 3.1 39.7 1.0 NZ A:LYS224 3.6 31.4 1.0 CD A:LYS224 3.7 34.3 1.0 O A:MET509 3.8 0.0 0.8 S2 A:SF4501 3.9 36.7 1.0 O A:SAH508 3.9 16.5 0.4 N A:CYS99 4.1 39.6 1.0 CA A:CYS99 4.2 40.2 1.0 CE A:LYS224 4.2 33.5 1.0 CB A:SER97 4.4 42.6 1.0 CB A:CYS102 4.7 34.1 1.0 O A:HOH670 4.7 36.3 1.0 SG A:CYS102 4.7 34.6 1.0 SG A:CYS95 4.7 33.5 1.0 N A:MET509 4.9 86.1 0.8 N A:SAH508 4.9 15.8 0.4 CG A:LYS224 4.9 36.6 1.0 C A:MET509 5.0 0.6 0.8

Iron binding site 3 out of 8 in the X-Ray Structure of the Tryptophan Lyase Nosl in Complex with (R)-(+)- Indoline-2-Carboxylate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of X-Ray Structure of the Tryptophan Lyase Nosl in Complex with (R)-(+)- Indoline-2-Carboxylate within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:36.2 occ:1.00 FE3 A:SF4501 0.0 36.2 1.0 S4 A:SF4501 2.3 36.0 1.0 S2 A:SF4501 2.3 36.7 1.0 S1 A:SF4501 2.3 38.2 1.0 SG A:CYS102 2.3 34.6 1.0 FE2 A:SF4501 2.7 36.0 1.0 FE1 A:SF4501 2.7 35.7 1.0 FE4 A:SF4501 2.8 35.6 1.0 CB A:CYS102 3.1 34.1 1.0 NE2 A:GLN363 3.8 31.9 1.0 S3 A:SF4501 3.9 36.5 1.0 CB A:MET104 4.2 32.5 1.0 CB A:CYS99 4.3 39.7 1.0 SD A:MET509 4.4 0.6 0.8 SG A:CYS99 4.6 38.9 1.0 CA A:CYS102 4.6 35.0 1.0 N A:ARG105 4.7 41.9 1.0 C A:MET104 4.8 37.6 1.0 N A:SAH508 4.8 15.8 0.4 CD A:GLN363 4.8 35.1 1.0 N A:MET509 4.8 86.1 0.8 N A:MET104 4.8 37.0 1.0 O A:SAH508 4.8 16.5 0.4 CA A:MET104 4.8 34.4 1.0 O A:MET509 4.8 0.0 0.8 CG A:SAH508 4.9 13.8 0.4 SG A:CYS95 4.9 33.5 1.0 CG A:GLN363 4.9 35.6 1.0 CE A:MET509 4.9 92.2 0.8

Iron binding site 4 out of 8 in the X-Ray Structure of the Tryptophan Lyase Nosl in Complex with (R)-(+)- Indoline-2-Carboxylate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of X-Ray Structure of the Tryptophan Lyase Nosl in Complex with (R)-(+)- Indoline-2-Carboxylate within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:35.6 occ:1.00 FE4 A:SF4501 0.0 35.6 1.0 O A:SAH508 2.2 16.5 0.4 O A:MET509 2.3 0.0 0.8 S2 A:SF4501 2.3 36.7 1.0 S3 A:SF4501 2.3 36.5 1.0 S1 A:SF4501 2.3 38.2 1.0 N A:MET509 2.3 86.1 0.8 N A:SAH508 2.4 15.8 0.4 FE2 A:SF4501 2.7 36.0 1.0 FE3 A:SF4501 2.8 36.2 1.0 FE1 A:SF4501 2.8 35.7 1.0 SD A:MET509 3.0 0.6 0.8 C A:SAH508 3.0 16.2 0.4 C A:MET509 3.0 0.6 0.8 CA A:SAH508 3.1 15.6 0.4 CA A:MET509 3.2 94.3 0.8 CG A:SAH508 3.3 13.8 0.4 CB A:SAH508 3.7 14.7 0.4 CG A:MET509 3.9 0.4 0.8 NZ A:LYS224 3.9 31.4 1.0 S4 A:SF4501 4.0 36.0 1.0 CE A:MET509 4.0 92.2 0.8 CB A:MET509 4.0 92.7 0.8 OXT A:SAH508 4.2 16.4 0.4 OXT A:MET509 4.2 0.3 0.8 CD A:LYS224 4.6 34.3 1.0 SG A:CYS95 4.7 33.5 1.0 NE2 A:GLN363 4.7 31.9 1.0 SD A:SAH508 4.8 20.8 0.4 SG A:CYS99 4.9 38.9 1.0 O A:THR141 4.9 27.6 1.0 SG A:CYS102 4.9 34.6 1.0 N A:GLU143 4.9 33.7 1.0 CA A:GLY142 4.9 30.6 1.0 CE A:LYS224 4.9 33.5 1.0

Iron binding site 5 out of 8 in the X-Ray Structure of the Tryptophan Lyase Nosl in Complex with (R)-(+)- Indoline-2-Carboxylate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of X-Ray Structure of the Tryptophan Lyase Nosl in Complex with (R)-(+)- Indoline-2-Carboxylate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:21.4 occ:1.00 FE1 B:SF4501 0.0 21.4 1.0 SG B:CYS102 2.3 23.1 1.0 S4 B:SF4501 2.3 23.0 1.0 S2 B:SF4501 2.3 21.1 1.0 S3 B:SF4501 2.3 20.9 1.0 FE3 B:SF4501 2.7 21.2 1.0 FE2 B:SF4501 2.7 22.1 1.0 FE4 B:SF4501 2.8 20.5 1.0 CB B:CYS102 3.2 20.0 1.0 S1 B:SF4501 3.9 18.7 1.0 NE2 B:GLN363 3.9 22.6 1.0 CB B:MET104 4.2 20.7 1.0 SD B:MET503 4.4 67.9 0.7 CB B:CYS99 4.4 20.5 1.0 SG B:CYS99 4.6 22.9 1.0 CA B:CYS102 4.6 22.2 1.0 N B:ARG105 4.7 27.7 1.0 C B:MET104 4.7 25.8 1.0 N B:MET104 4.8 27.1 1.0 O B:SAH502 4.8 16.3 0.6 CA B:MET104 4.8 26.4 1.0 N B:SAH502 4.8 15.8 0.6 O B:MET503 4.8 80.2 0.7 CG B:SAH502 4.8 10.6 0.6 N B:MET503 4.8 71.2 0.7 SG B:CYS95 4.9 20.7 1.0 CD B:GLN363 4.9 21.4 1.0

Iron binding site 6 out of 8 in the X-Ray Structure of the Tryptophan Lyase Nosl in Complex with (R)-(+)- Indoline-2-Carboxylate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of X-Ray Structure of the Tryptophan Lyase Nosl in Complex with (R)-(+)- Indoline-2-Carboxylate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:22.1 occ:1.00 FE2 B:SF4501 0.0 22.1 1.0 S3 B:SF4501 2.3 20.9 1.0 SG B:CYS95 2.3 20.7 1.0 S1 B:SF4501 2.3 18.7 1.0 S4 B:SF4501 2.3 23.0 1.0 FE1 B:SF4501 2.7 21.4 1.0 FE3 B:SF4501 2.7 21.2 1.0 FE4 B:SF4501 2.8 20.5 1.0 CB B:CYS95 3.4 20.6 1.0 S2 B:SF4501 3.9 21.1 1.0 N B:MET503 4.0 71.2 0.7 CB B:SER97 4.1 24.7 1.0 N B:SAH502 4.1 15.8 0.6 N B:GLU143 4.4 20.8 1.0 CA B:GLY142 4.5 17.7 1.0 O B:MET503 4.7 80.2 0.7 O B:MET104 4.7 27.2 1.0 N B:SER97 4.7 22.3 1.0 SG B:CYS102 4.8 23.1 1.0 CA B:SER97 4.8 23.2 1.0 O B:SAH502 4.8 16.3 0.6 SG B:CYS99 4.8 22.9 1.0 C B:SER97 4.8 24.7 1.0 CA B:CYS95 4.8 22.2 1.0 O B:SER97 4.8 24.0 1.0 CB B:MET104 4.9 20.7 1.0 C B:MET104 4.9 25.8 1.0 C B:GLY142 5.0 18.5 1.0

Iron binding site 7 out of 8 in the X-Ray Structure of the Tryptophan Lyase Nosl in Complex with (R)-(+)- Indoline-2-Carboxylate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of X-Ray Structure of the Tryptophan Lyase Nosl in Complex with (R)-(+)- Indoline-2-Carboxylate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:21.2 occ:1.00 FE3 B:SF4501 0.0 21.2 1.0 S1 B:SF4501 2.3 18.7 1.0 SG B:CYS99 2.3 22.9 1.0 S2 B:SF4501 2.3 21.1 1.0 S4 B:SF4501 2.3 23.0 1.0 FE1 B:SF4501 2.7 21.4 1.0 FE2 B:SF4501 2.7 22.1 1.0 FE4 B:SF4501 2.7 20.5 1.0 CB B:CYS99 3.1 20.5 1.0 CD B:LYS224 3.8 21.1 1.0 NZ B:LYS224 3.8 18.9 1.0 S3 B:SF4501 3.9 20.9 1.0 O B:MET503 3.9 80.2 0.7 O B:SAH502 4.0 16.3 0.6 N B:CYS99 4.1 23.0 1.0 CA B:CYS99 4.2 23.5 1.0 CE B:LYS224 4.3 19.5 1.0 CB B:SER97 4.4 24.7 1.0 O B:HOH747 4.6 23.0 1.0 CB B:CYS102 4.6 20.0 1.0 SG B:CYS102 4.7 23.1 1.0 SG B:CYS95 4.7 20.7 1.0 N B:MET503 4.9 71.2 0.7 N B:SAH502 5.0 15.8 0.6

Iron binding site 8 out of 8 in the X-Ray Structure of the Tryptophan Lyase Nosl in Complex with (R)-(+)- Indoline-2-Carboxylate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of X-Ray Structure of the Tryptophan Lyase Nosl in Complex with (R)-(+)- Indoline-2-Carboxylate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:20.5 occ:1.00 FE4 B:SF4501 0.0 20.5 1.0 O B:SAH502 2.2 16.3 0.6 O B:MET503 2.3 80.2 0.7 S2 B:SF4501 2.3 21.1 1.0 S1 B:SF4501 2.3 18.7 1.0 S3 B:SF4501 2.3 20.9 1.0 N B:MET503 2.4 71.2 0.7 N B:SAH502 2.4 15.8 0.6 FE3 B:SF4501 2.7 21.2 1.0 FE2 B:SF4501 2.8 22.1 1.0 FE1 B:SF4501 2.8 21.4 1.0 SD B:MET503 3.0 67.9 0.7 C B:SAH502 3.0 15.3 0.6 C B:MET503 3.0 78.5 0.7 CA B:SAH502 3.1 14.5 0.6 CA B:MET503 3.2 73.0 0.7 CG B:SAH502 3.3 10.6 0.6 CB B:SAH502 3.7 11.4 0.6 CG B:MET503 3.9 68.3 0.7 CE B:MET503 4.0 65.2 0.7 S4 B:SF4501 4.0 23.0 1.0 CB B:MET503 4.0 66.7 0.7 NZ B:LYS224 4.1 18.9 1.0 OXT B:SAH502 4.2 16.0 0.6 OXT B:MET503 4.2 81.0 0.7 CD B:LYS224 4.6 21.1 1.0 SG B:CYS95 4.7 20.7 1.0 NE2 B:GLN363 4.8 22.6 1.0 O B:THR141 4.8 15.7 1.0 SD B:SAH502 4.8 18.9 0.6 SG B:CYS99 4.9 22.9 1.0 CA B:GLY142 4.9 17.7 1.0 SG B:CYS102 4.9 23.1 1.0 N B:GLU143 5.0 20.8 1.0

P.Amara, J.M.Mouesca, M.Bella, L.Martin, C.Saragaglia, S.Gambarelli, Y.Nicolet. Radical S-Adenosyl-L-Methionine Tryptophan Lyase (Nosl): How the Protein Controls the Carboxyl Radical •CO2-Migration. J.Am.Chem.Soc. V. 140 16661 2018.
ISSN: ESSN 1520-5126
PubMed: 30418774
DOI: 10.1021/JACS.8B09142