Iodine in PDB 1nlu: Pseudomonas Sedolisin (Serine-Carboxyl Proteinase) Complexed with Two Molecules of Pseudo-Iodotyrostatin

All present enzymatic activity of Pseudomonas Sedolisin (Serine-Carboxyl Proteinase) Complexed with Two Molecules of Pseudo-Iodotyrostatin:
3.4.21.100;

The structure of Pseudomonas Sedolisin (Serine-Carboxyl Proteinase) Complexed with Two Molecules of Pseudo-Iodotyrostatin, PDB code: 1nlu was solved by A.Wlodawer, M.Li, A.Gustchina, Z.Dauter, K.Uchida, H.Oyama, N.E.Glodfarb, B.M.Dunn, K.Oda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.30
Space group	P 62
Cell size a, b, c (Å), α, β, γ (°)	97.840, 97.840, 82.680, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / 19.5

The structure of Pseudomonas Sedolisin (Serine-Carboxyl Proteinase) Complexed with Two Molecules of Pseudo-Iodotyrostatin also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

The binding sites of Iodine atom in the Pseudomonas Sedolisin (Serine-Carboxyl Proteinase) Complexed with Two Molecules of Pseudo-Iodotyrostatin (pdb code 1nlu). This binding sites where shown within 5.0 Angstroms radius around Iodine atom.
In total 2 binding sites of Iodine where determined in the Pseudomonas Sedolisin (Serine-Carboxyl Proteinase) Complexed with Two Molecules of Pseudo-Iodotyrostatin, PDB code: 1nlu:
Jump to Iodine binding site number: 1; 2;

Iodine binding site 1 out of 2 in the Pseudomonas Sedolisin (Serine-Carboxyl Proteinase) Complexed with Two Molecules of Pseudo-Iodotyrostatin


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 1 of Pseudomonas Sedolisin (Serine-Carboxyl Proteinase) Complexed with Two Molecules of Pseudo-Iodotyrostatin within 5.0Å range: probe atom residue distance (Å) B Occ B:I2 b:15.9 occ:0.50 I B:PHI2 0.0 15.9 0.5 CZ B:PHI2 2.0 18.6 1.0 CE2 B:PHI2 2.9 21.3 1.0 CE1 B:PHI2 3.0 22.7 1.0 CG A:ASP74 3.5 16.6 1.0 O A:HOH704 3.6 27.9 1.0 OD2 A:ASP74 3.7 18.6 1.0 OD1 A:ASP74 3.8 22.4 1.0 CB A:ASP74 3.8 15.2 1.0 CG2 A:ILE35 3.9 12.5 1.0 CB A:ILE35 4.0 12.3 1.0 CD2 B:PHI2 4.2 19.2 1.0 O A:ILE35 4.2 11.6 1.0 CA A:GLY77 4.3 12.9 1.0 CD1 B:PHI2 4.3 23.9 1.0 CZ2 A:TRP81 4.5 10.6 1.0 N A:GLY77 4.6 14.1 1.0 CG B:PHI2 4.8 12.9 1.0 O A:HOH945 4.9 50.0 1.0 CG1 A:ILE35 4.9 15.0 1.0 C A:ILE35 5.0 9.6 1.0 CD1 A:ILE35 5.0 40.6 1.0

Iodine binding site 2 out of 2 in the Pseudomonas Sedolisin (Serine-Carboxyl Proteinase) Complexed with Two Molecules of Pseudo-Iodotyrostatin


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 2 of Pseudomonas Sedolisin (Serine-Carboxyl Proteinase) Complexed with Two Molecules of Pseudo-Iodotyrostatin within 5.0Å range: probe atom residue distance (Å) B Occ C:I2 b:21.6 occ:0.50 I C:PHI2 0.0 21.6 0.5 CZ C:PHI2 2.0 21.6 1.0 CE2 C:PHI2 3.0 21.4 1.0 CE1 C:PHI2 3.0 16.9 1.0 CD1 A:TRP231 3.8 15.7 1.0 O A:HOH731 4.0 27.6 1.0 O A:GLU222 4.1 14.7 1.0 CG A:TRP231 4.2 12.9 1.0 CD2 C:PHI2 4.3 17.8 1.0 CB A:TRP231 4.3 11.7 1.0 CB A:ASP225 4.3 19.2 1.0 CD1 C:PHI2 4.3 16.1 1.0 CB A:GLU222 4.4 11.8 1.0 CA A:ASP225 4.4 18.3 1.0 O A:LEU224 4.5 19.9 1.0 N A:ASP225 4.5 16.5 1.0 NE1 A:TRP231 4.6 15.6 1.0 C A:LEU224 4.6 15.6 1.0 O C:HOH360 4.6 52.6 1.0 O A:GLY223 4.6 14.1 1.0 O A:HOH873 4.7 34.8 1.0 C A:GLU222 4.7 11.7 1.0 CG C:PHI2 4.9 17.2 1.0 O A:HOH755 5.0 46.6 1.0

A.Wlodawer, M.Li, A.Gustchina, H.Oyama, K.Oda, B.B.Beyer, J.Clemente, B.M.Dunn. Two Inhibitor Molecules Bound in the Active Site of Pseudomonas Sedolisin: A Model For the Bi-Product Complex Following Cleavage of A Peptide Substrate. Biochem.Biophys.Res.Commun. V. 314 638 2004.
ISSN: ISSN 0006-291X
PubMed: 14733955
DOI: 10.1016/J.BBRC.2003.12.130