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

Protein crystallography data

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

Other elements in 6htk:

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

Iron Binding Sites:

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 6htk

Go back to Iron Binding Sites List in 6htk
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 6htk

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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 6htk

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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 6htk

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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 6htk

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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 6htk

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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 6htk

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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 6htk

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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

Reference:

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
Page generated: Wed Aug 6 07:55:26 2025

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