Iron in PDB 8vyy: The Crystal Structure of Mare in Complex with Its Native Substrate, Beta-Methyl-L-Tryptophan

The structure of The Crystal Structure of Mare in Complex with Its Native Substrate, Beta-Methyl-L-Tryptophan, PDB code: 8vyy was solved by I.Shin, A.Liu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.85 / 2.45
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	196.119, 196.119, 113.06, 90, 90, 90
R / Rfree (%)	17.7 / 21

The binding sites of Iron atom in the The Crystal Structure of Mare in Complex with Its Native Substrate, Beta-Methyl-L-Tryptophan (pdb code 8vyy). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the The Crystal Structure of Mare in Complex with Its Native Substrate, Beta-Methyl-L-Tryptophan, PDB code: 8vyy:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the The Crystal Structure of Mare in Complex with Its Native Substrate, Beta-Methyl-L-Tryptophan


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Crystal Structure of Mare in Complex with Its Native Substrate, Beta-Methyl-L-Tryptophan within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe301 b:42.4 occ:1.00 FE A:HEM301 0.0 42.4 1.0 NC A:HEM301 2.0 47.5 1.0 ND A:HEM301 2.1 53.8 1.0 NA A:HEM301 2.1 41.5 1.0 NE2 A:HIS201 2.1 44.2 1.0 NB A:HEM301 2.1 41.9 1.0 CE1 A:HIS201 3.0 42.7 1.0 C4C A:HEM301 3.0 53.1 1.0 C1C A:HEM301 3.0 50.2 1.0 C1D A:HEM301 3.0 50.1 1.0 C4D A:HEM301 3.1 48.5 1.0 C1A A:HEM301 3.1 46.6 1.0 C4A A:HEM301 3.1 42.6 1.0 C1B A:HEM301 3.2 43.3 1.0 C4B A:HEM301 3.2 41.2 1.0 CD2 A:HIS201 3.2 42.6 1.0 CHD A:HEM301 3.4 44.1 1.0 CHC A:HEM301 3.5 44.6 1.0 CHA A:HEM301 3.5 49.1 1.0 CHB A:HEM301 3.5 42.5 1.0 CD1 A:78U302 3.6 54.3 0.6 ND1 A:HIS201 4.1 42.0 1.0 C3C A:HEM301 4.2 43.0 1.0 C2C A:HEM301 4.2 49.3 1.0 CG A:HIS201 4.2 43.4 1.0 C2D A:HEM301 4.3 55.8 1.0 NE1 A:78U302 4.3 50.6 0.6 C3D A:HEM301 4.3 53.4 1.0 C3A A:HEM301 4.3 42.7 1.0 C2A A:HEM301 4.3 40.6 1.0 C2B A:HEM301 4.4 42.2 1.0 C3B A:HEM301 4.4 45.4 1.0 CAG A:78U302 4.4 54.0 0.6 CD1 A:78U302 4.5 55.1 0.1 CB A:78U302 4.5 59.0 0.6 NE1 A:78U302 4.5 53.2 0.1 CE A:MET204 4.7 50.2 1.0 CG A:78U302 4.7 59.2 0.6 CA A:GLY127 5.0 42.1 1.0

Iron binding site 2 out of 2 in the The Crystal Structure of Mare in Complex with Its Native Substrate, Beta-Methyl-L-Tryptophan


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of The Crystal Structure of Mare in Complex with Its Native Substrate, Beta-Methyl-L-Tryptophan within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe301 b:41.0 occ:1.00 FE B:HEM301 0.0 41.0 1.0 NC B:HEM301 2.0 47.8 1.0 NB B:HEM301 2.1 42.7 1.0 NA B:HEM301 2.1 44.3 1.0 ND B:HEM301 2.1 48.8 1.0 NE2 B:HIS201 2.1 37.0 1.0 CE1 B:HIS201 3.0 43.0 1.0 C1C B:HEM301 3.0 46.9 1.0 C4C B:HEM301 3.0 49.6 1.0 C4B B:HEM301 3.1 44.2 1.0 C4A B:HEM301 3.1 41.7 1.0 C1B B:HEM301 3.1 45.0 1.0 C4D B:HEM301 3.1 47.8 1.0 C1A B:HEM301 3.1 46.7 1.0 C1D B:HEM301 3.1 50.8 1.0 CD2 B:HIS201 3.2 41.5 1.0 CHC B:HEM301 3.4 43.0 1.0 CD1 B:78U302 3.5 62.6 0.8 CHB B:HEM301 3.5 43.4 1.0 CHD B:HEM301 3.5 45.2 1.0 CHA B:HEM301 3.5 51.6 1.0 NE1 B:78U302 4.1 57.3 0.8 ND1 B:HIS201 4.2 35.0 1.0 C3C B:HEM301 4.3 49.4 1.0 C2C B:HEM301 4.3 50.7 1.0 C3A B:HEM301 4.3 52.8 1.0 CG B:HIS201 4.3 41.5 1.0 C3B B:HEM301 4.3 41.5 1.0 C2A B:HEM301 4.3 46.9 1.0 C2B B:HEM301 4.3 45.4 1.0 C3D B:HEM301 4.3 46.4 1.0 C2D B:HEM301 4.3 54.0 1.0 CAG B:78U302 4.4 60.9 0.8 CB B:78U302 4.5 70.8 0.8 CG B:78U302 4.7 73.2 0.8 CE B:MET204 4.8 51.7 1.0

I.Shin, R.C.Nguyen, S.R.Montoya, A.Liu. Structural Insights Into 2-Oxindole-Forming Monooxygenase Mare: Divergent Architecture and Substrate Positioning Versus Tryptophan Dioxygenases. J.Biol.Chem. V. 301 08241 2025.
ISSN: ESSN 1083-351X
PubMed: 39880093
DOI: 10.1016/J.JBC.2025.108241