Chlorine in PDB 3i2a: Crystal Structure of A Chimeric Trypsin Inhibitor Protein Sti(L)- Wci(S)

The structure of Crystal Structure of A Chimeric Trypsin Inhibitor Protein Sti(L)- Wci(S), PDB code: 3i2a was solved by U.Sen, S.Khamrui, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.96 / 2.30
Space group	I 4
Cell size a, b, c (Å), α, β, γ (°)	141.383, 141.383, 46.716, 90.00, 90.00, 90.00
R / Rfree (%)	23.4 / 28.9

The binding sites of Chlorine atom in the Crystal Structure of A Chimeric Trypsin Inhibitor Protein Sti(L)- Wci(S) (pdb code 3i2a). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of A Chimeric Trypsin Inhibitor Protein Sti(L)- Wci(S), PDB code: 3i2a:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of A Chimeric Trypsin Inhibitor Protein Sti(L)- Wci(S)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of A Chimeric Trypsin Inhibitor Protein Sti(L)- Wci(S) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl402 b:36.7 occ:1.00 NE A:ARG50 3.2 34.9 1.0 NH1 A:ARG161 3.3 35.5 1.0 NH1 A:ARG155 3.3 40.7 1.0 CD A:ARG161 3.4 36.7 1.0 NH2 A:ARG50 3.5 35.2 1.0 CZ A:ARG50 3.8 35.9 1.0 CD1 A:ILE153 3.8 37.8 1.0 CZ A:ARG161 4.0 37.2 1.0 NE A:ARG161 4.0 38.3 1.0 CG A:ARG50 4.1 34.3 1.0 CD A:ARG50 4.2 34.2 1.0 CB A:ALA29 4.2 19.8 1.0 CG A:ARG161 4.3 34.3 1.0 CG2 A:ILE153 4.5 41.3 1.0 CB A:ARG161 4.5 32.8 1.0 CZ A:ARG155 4.5 45.4 1.0 CD1 A:ILE27 4.6 20.5 1.0 CH2 B:TRP228 4.7 31.9 1.0 O A:HIS30 4.7 34.1 1.0 CZ2 B:TRP228 4.9 30.1 1.0 CD A:ARG155 4.9 43.3 1.0 CG1 A:ILE153 5.0 40.0 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of A Chimeric Trypsin Inhibitor Protein Sti(L)- Wci(S)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of A Chimeric Trypsin Inhibitor Protein Sti(L)- Wci(S) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl401 b:32.9 occ:1.00 NH2 B:ARG250 3.1 26.5 1.0 O B:HOH431 3.2 37.6 1.0 N B:GLU372 3.2 25.5 1.0 NH1 B:ARG250 3.3 26.2 1.0 ND1 B:HIS230 3.3 35.7 1.0 O B:HOH440 3.3 44.7 1.0 CZ B:ARG250 3.6 27.8 1.0 O B:GLU372 3.6 27.9 1.0 CB B:PRO225 3.7 18.0 1.0 CA B:LEU371 3.8 29.0 1.0 O B:PRO370 4.0 44.5 1.0 C B:LEU371 4.0 28.4 1.0 C B:GLU372 4.0 26.8 1.0 CE1 B:HIS230 4.1 35.1 1.0 CA B:PRO225 4.1 23.1 1.0 CA B:GLU372 4.1 27.9 1.0 CG B:HIS230 4.3 32.4 1.0 CD2 B:LEU371 4.3 26.7 1.0 CB B:GLU372 4.4 35.6 1.0 CB B:HIS230 4.6 29.4 1.0 CB B:LEU371 4.6 28.4 1.0 CD2 B:LEU373 4.7 22.1 1.0 O B:HOH518 4.8 47.2 1.0 N B:LEU371 4.8 32.8 1.0 C B:PRO370 4.8 43.2 1.0 NE B:ARG250 4.8 26.3 1.0 N B:HIS226 4.8 26.7 1.0 N B:LEU373 5.0 31.9 1.0 C B:PRO225 5.0 23.5 1.0

S.Khamrui, S.Majumder, J.Dasgupta, J.K.Dattagupta, U.Sen. Identification of A Novel Set of Scaffolding Residues That Are Instrumental For the Inhibitory Property of Kunitz (Sti) Inhibitors. Protein Sci. V. 19 593 2010.
ISSN: ISSN 0961-8368
PubMed: 20073082
DOI: 10.1002/PRO.338