Iodine in PDB 5ncw: Structure of the Trypsin Induced Serpin-Type Proteinase Inhibitor, Miropin (V367K/K368A Mutant).

The structure of Structure of the Trypsin Induced Serpin-Type Proteinase Inhibitor, Miropin (V367K/K368A Mutant)., PDB code: 5ncw was solved by T.Goulas, M.Ksiazek, I.Garcia-Ferrer, D.Mizgalska, J.Potempa, X.Gomis-Ruth, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	55.75 / 1.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	62.600, 74.280, 84.380, 90.00, 90.00, 90.00
R / Rfree (%)	16.3 / 18.3

The structure of Structure of the Trypsin Induced Serpin-Type Proteinase Inhibitor, Miropin (V367K/K368A Mutant). also contains other interesting chemical elements:

Potassium	(K)	1 atom
Zinc	(Zn)	2 atoms
Chlorine	(Cl)	6 atoms

The binding sites of Iodine atom in the Structure of the Trypsin Induced Serpin-Type Proteinase Inhibitor, Miropin (V367K/K368A Mutant). (pdb code 5ncw). This binding sites where shown within 5.0 Angstroms radius around Iodine atom.
In total 4 binding sites of Iodine where determined in the Structure of the Trypsin Induced Serpin-Type Proteinase Inhibitor, Miropin (V367K/K368A Mutant)., PDB code: 5ncw:
Jump to Iodine binding site number: 1; 2; 3; 4;

Iodine binding site 1 out of 4 in the Structure of the Trypsin Induced Serpin-Type Proteinase Inhibitor, Miropin (V367K/K368A Mutant).


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 1 of Structure of the Trypsin Induced Serpin-Type Proteinase Inhibitor, Miropin (V367K/K368A Mutant). within 5.0Å range: probe atom residue distance (Å) B Occ A:I504 b:22.8 occ:0.44 O A:HOH795 3.5 20.8 0.5 NZ A:LYS52 3.6 28.8 1.0 O A:HOH934 3.7 44.1 1.0 O A:TYR60 3.9 19.7 1.0 C A:TYR60 4.2 19.9 1.0 CA A:THR61 4.2 17.6 1.0 CG2 A:THR61 4.4 20.3 1.0 N A:THR61 4.4 17.4 1.0 CB A:THR61 4.9 21.1 1.0 C A:GLY59 4.9 24.9 1.0 N A:TYR60 4.9 19.9 1.0

Iodine binding site 2 out of 4 in the Structure of the Trypsin Induced Serpin-Type Proteinase Inhibitor, Miropin (V367K/K368A Mutant).


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 2 of Structure of the Trypsin Induced Serpin-Type Proteinase Inhibitor, Miropin (V367K/K368A Mutant). within 5.0Å range: probe atom residue distance (Å) B Occ A:I505 b:17.3 occ:0.39 O A:HOH657 3.3 33.3 1.0 N A:ILE148 3.7 18.7 1.0 O A:ILE148 4.2 21.0 1.0 CA A:TYR147 4.2 18.0 1.0 O A:HOH874 4.4 44.7 1.0 CD2 A:LEU126 4.4 24.4 1.0 C A:TYR147 4.5 20.6 1.0 O A:HOH844 4.5 18.5 0.5 CB A:ILE148 4.5 20.3 1.0 CA A:ILE148 4.5 17.3 1.0 CB A:TYR147 4.6 20.4 1.0 O A:HOH612 4.7 33.7 1.0 O A:HOH658 4.8 17.5 1.0 C A:ILE148 4.8 19.5 1.0 O A:HOH951 4.9 24.4 1.0 CG1 A:ILE148 4.9 21.5 1.0

Iodine binding site 3 out of 4 in the Structure of the Trypsin Induced Serpin-Type Proteinase Inhibitor, Miropin (V367K/K368A Mutant).


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 3 of Structure of the Trypsin Induced Serpin-Type Proteinase Inhibitor, Miropin (V367K/K368A Mutant). within 5.0Å range: probe atom residue distance (Å) B Occ A:I506 b:24.8 occ:0.44 O A:HOH674 3.2 25.7 1.0 O A:HOH995 3.8 34.8 1.0 ND2 B:ASN382 3.9 29.6 1.0 CB A:ARG259 4.1 17.3 1.0 CE A:MET192 4.1 16.9 1.0 CG A:ARG259 4.2 24.0 1.0 CB B:ASN382 4.3 17.9 1.0 CG A:MET192 4.3 17.5 1.0 CB B:HIS380 4.4 19.6 1.0 CG B:ASN382 4.6 24.1 1.0 ND1 B:HIS380 4.6 26.3 1.0 SD A:MET192 4.6 18.4 1.0 CG B:HIS380 4.7 23.5 1.0 CB A:ALA178 4.8 19.9 1.0 CD A:ARG259 4.8 32.8 1.0

Iodine binding site 4 out of 4 in the Structure of the Trypsin Induced Serpin-Type Proteinase Inhibitor, Miropin (V367K/K368A Mutant).


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 4 of Structure of the Trypsin Induced Serpin-Type Proteinase Inhibitor, Miropin (V367K/K368A Mutant). within 5.0Å range: probe atom residue distance (Å) B Occ A:I507 b:19.6 occ:0.28 SD A:MET34 3.2 19.6 0.3 OG A:SER69 3.4 16.8 0.3 OG A:SER69 3.5 14.5 0.7 CG A:MET34 3.6 15.6 0.3 OG A:SER33 3.6 16.3 0.7 OG A:SER33 3.7 20.3 0.3 OD1 A:ASN37 3.7 16.7 1.0 CE A:MET34 3.9 15.2 0.7 CB A:SER69 4.1 15.1 0.3 N A:MET34 4.1 12.2 1.0 CA A:MET34 4.1 11.3 0.7 CB A:SER33 4.1 13.1 0.3 CA A:MET34 4.1 11.3 0.3 CB A:SER69 4.1 14.2 0.7 CB A:MET34 4.3 12.3 0.7 C A:SER33 4.3 14.2 1.0 CD1 A:LEU30 4.4 21.3 1.0 CB A:SER33 4.4 16.7 0.7 CB A:MET34 4.5 12.9 0.3 CA A:SER69 4.5 13.8 0.7 O A:SER33 4.5 12.8 1.0 CA A:SER69 4.6 13.5 0.3 CD2 A:LEU72 4.6 23.1 1.0 O A:LEU30 4.7 13.8 1.0 CG A:MET34 4.7 14.0 0.7 CG A:ASN37 4.8 14.2 1.0 O A:HOH834 4.9 36.4 1.0 CA A:SER33 4.9 11.6 0.3 CE A:MET34 5.0 17.5 0.3

T.Goulas, M.Ksiazek, I.Garcia-Ferrer, A.M.Sochaj-Gregorczyk, I.Waligorska, M.Wasylewski, J.Potempa, F.X.Gomis-Ruth. A Structure-Derived Snap-Trap Mechanism of A Multispecific Serpin From the Dysbiotic Human Oral Microbiome. J. Biol. Chem. V. 292 10883 2017.
ISSN: ESSN 1083-351X
PubMed: 28512127
DOI: 10.1074/JBC.M117.786533