Chlorine in PDB 2f91: 1.2A Resolution Structure of A Crayfish Trypsin Complexed with A Peptide Inhibitor, Sgti

All present enzymatic activity of 1.2A Resolution Structure of A Crayfish Trypsin Complexed with A Peptide Inhibitor, Sgti:
3.4.21.4;

The structure of 1.2A Resolution Structure of A Crayfish Trypsin Complexed with A Peptide Inhibitor, Sgti, PDB code: 2f91 was solved by K.Fodor, V.Harmat, C.Hetenyi, J.Kardos, J.Antal, A.Perczel, A.Patthy, G.Katona, L.Graf, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.10 / 1.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	41.283, 59.673, 97.302, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / 18.2

The structure of 1.2A Resolution Structure of A Crayfish Trypsin Complexed with A Peptide Inhibitor, Sgti also contains other interesting chemical elements:

Cadmium

(Cd)

6 atoms

The binding sites of Chlorine atom in the 1.2A Resolution Structure of A Crayfish Trypsin Complexed with A Peptide Inhibitor, Sgti (pdb code 2f91). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the 1.2A Resolution Structure of A Crayfish Trypsin Complexed with A Peptide Inhibitor, Sgti, PDB code: 2f91:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the 1.2A Resolution Structure of A Crayfish Trypsin Complexed with A Peptide Inhibitor, Sgti


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of 1.2A Resolution Structure of A Crayfish Trypsin Complexed with A Peptide Inhibitor, Sgti within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl407 b:11.4 occ:0.80 CD A:CD402 2.6 7.6 0.8 O A:HOH725 3.2 26.7 0.5 OD2 A:ASP135 3.7 11.4 1.0 CL A:CL408 3.9 11.8 0.8 O A:HOH620 4.0 27.7 1.0 O A:HOH655 4.1 27.6 1.0 CG A:ASP135 4.7 8.2 1.0 OD1 A:ASP135 4.9 8.9 1.0

Chlorine binding site 2 out of 2 in the 1.2A Resolution Structure of A Crayfish Trypsin Complexed with A Peptide Inhibitor, Sgti


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of 1.2A Resolution Structure of A Crayfish Trypsin Complexed with A Peptide Inhibitor, Sgti within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl408 b:11.8 occ:0.80 CD A:CD402 2.4 7.6 0.8 HZ1 A:LYS188 2.5 33.4 1.0 HD3 A:PRO161 2.8 10.8 1.0 HA A:VAL160 3.0 9.8 1.0 O A:HOH620 3.2 27.7 1.0 HG23 A:THR159 3.2 17.0 1.0 NZ A:LYS188 3.3 22.2 1.0 O A:THR159 3.4 10.0 1.0 HZ3 A:LYS188 3.5 33.4 1.0 OD2 A:ASP135 3.7 11.4 1.0 CD A:PRO161 3.7 9.0 1.0 HE3 A:LYS188 3.7 30.4 1.0 CA A:VAL160 3.8 8.2 1.0 C A:THR159 3.8 8.9 1.0 OD1 A:ASP135 3.8 8.9 1.0 O A:HOH725 3.9 26.7 0.5 CL A:CL407 3.9 11.4 0.8 HG11 A:VAL185 4.0 17.6 1.0 HG12 A:VAL185 4.0 17.6 1.0 HZ2 A:LYS188 4.0 33.4 1.0 CG A:ASP135 4.0 8.2 1.0 CE A:LYS188 4.0 25.3 1.0 N A:VAL160 4.0 8.7 1.0 N A:PRO161 4.1 8.0 1.0 CG2 A:THR159 4.1 11.3 1.0 C A:VAL160 4.1 7.6 1.0 HD2 A:PRO161 4.1 10.8 1.0 HB A:THR159 4.2 12.6 1.0 HE2 A:LYS188 4.2 30.4 1.0 CG1 A:VAL185 4.3 11.8 1.0 HG21 A:THR159 4.3 17.0 1.0 HG13 A:VAL185 4.3 17.6 1.0 CB A:THR159 4.5 10.5 1.0 HB3 A:PRO161 4.6 9.8 1.0 HG3 A:PRO161 4.6 10.6 1.0 H A:VAL160 4.6 10.4 1.0 CG A:PRO161 4.7 8.8 1.0 HG22 A:THR159 4.8 17.0 1.0 CA A:THR159 4.8 9.5 1.0 HG11 A:VAL160 4.8 18.6 1.0 O A:HOH655 4.9 27.6 1.0 HB3 A:ASP135 4.9 10.6 1.0 O A:VAL160 4.9 8.4 1.0

K.Fodor, V.Harmat, R.Neutze, L.Szilagyi, L.Graf, G.Katona. Enzyme:Substrate Hydrogen Bond Shortening During the Acylation Phase of Serine Protease Catalysis. Biochemistry V. 45 2114 2006.
ISSN: ISSN 0006-2960
PubMed: 16475800
DOI: 10.1021/BI0517133