Chlorine in PDB 4oem: Crystal Structure of Cathepsin C in Complex with Dipeptide Substrates

All present enzymatic activity of Crystal Structure of Cathepsin C in Complex with Dipeptide Substrates:
3.4.14.1;

The structure of Crystal Structure of Cathepsin C in Complex with Dipeptide Substrates, PDB code: 4oem was solved by B.Zhao, A.Smallwood, N.Concha, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.49 / 1.52
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	84.920, 89.016, 115.098, 90.00, 90.00, 90.00
R / Rfree (%)	16.4 / 17.8

The binding sites of Chlorine atom in the Crystal Structure of Cathepsin C in Complex with Dipeptide Substrates (pdb code 4oem). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Cathepsin C in Complex with Dipeptide Substrates, PDB code: 4oem:

Chlorine binding site 1 out of 1 in the Crystal Structure of Cathepsin C in Complex with Dipeptide Substrates


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 Cathepsin C in Complex with Dipeptide Substrates within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl507 b:16.5 occ:1.00 HH A:TYR323 2.2 16.9 1.0 H A:TYR280 2.3 16.5 1.0 HB3 A:PHE278 2.6 16.2 1.0 HD2 A:PRO279 2.8 17.6 1.0 HG21 B:VAL431 2.9 22.4 1.0 HD2 A:PHE278 2.9 21.8 1.0 HE1 A:TYR323 2.9 17.2 1.0 HB2 A:TYR280 3.0 16.4 1.0 OH A:TYR323 3.2 17.5 1.0 O B:HOH512 3.2 25.5 1.0 N A:TYR280 3.3 14.7 1.0 HG12 B:ILE429 3.3 19.8 1.0 HB3 A:TYR280 3.4 14.7 1.0 O B:HOH546 3.5 27.3 1.0 HD11 B:ILE429 3.6 23.7 1.0 CB A:PHE278 3.6 16.9 1.0 CB A:TYR280 3.6 15.0 1.0 HD13 B:ILE429 3.6 21.7 1.0 CE1 A:TYR323 3.6 14.3 1.0 CD A:PRO279 3.7 16.6 1.0 N A:PRO279 3.7 15.6 1.0 HB2 A:PRO279 3.7 16.2 1.0 CG2 B:VAL431 3.7 21.9 1.0 CD2 A:PHE278 3.8 21.1 1.0 HG23 B:VAL431 3.8 24.2 1.0 CZ A:TYR323 3.8 14.7 1.0 CD1 B:ILE429 4.0 21.3 1.0 HA A:PHE278 4.0 14.8 1.0 C A:PHE278 4.0 16.8 1.0 HG22 B:VAL431 4.0 20.4 1.0 CA A:TYR280 4.1 14.4 1.0 CG1 B:ILE429 4.1 16.8 1.0 CA A:PHE278 4.1 15.9 1.0 HG23 A:ILE63 4.1 17.7 1.0 CG A:PHE278 4.2 18.0 1.0 C A:PRO279 4.2 15.8 1.0 CA A:PRO279 4.3 14.9 1.0 HB2 A:PHE278 4.4 16.3 1.0 CB A:PRO279 4.4 16.4 1.0 HG13 B:ILE429 4.4 17.9 1.0 HD3 A:PRO279 4.5 17.4 1.0 CG A:PRO279 4.5 19.3 1.0 HG2 A:PRO279 4.5 20.5 1.0 H A:LEU281 4.6 13.9 1.0 HA A:TYR280 4.7 12.7 1.0 O A:PHE278 4.7 16.6 1.0 HB2 A:TYR64 4.8 18.7 1.0 CD1 A:TYR323 4.8 15.8 1.0 HG11 B:VAL431 4.9 21.4 1.0 O B:ILE429 4.9 18.6 1.0 HB B:VAL431 5.0 20.7 1.0 CB B:VAL431 5.0 21.3 1.0 CG A:TYR280 5.0 15.3 1.0

J.K.Rubach, G.Cui, J.L.Schneck, A.N.Taylor, B.Zhao, A.Smallwood, N.Nevins, D.Wisnoski, S.H.Thrall, T.D.Meek. The Amino-Acid Substituents of Dipeptide Substrates of Cathepsin C Can Determine the Rate-Limiting Steps of Catalysis. Biochemistry V. 51 7551 2012.
ISSN: ISSN 0006-2960
PubMed: 22928782
DOI: 10.1021/BI300719B