Chlorine in PDB 6fzv: Crystal Structure of the Metalloproteinase Enhancer Pcpe-1 Bound to the Procollagen C Propeptide Trimer (Short)

The structure of Crystal Structure of the Metalloproteinase Enhancer Pcpe-1 Bound to the Procollagen C Propeptide Trimer (Short), PDB code: 6fzv was solved by D.Pulido, E.Hohenester, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	79.37 / 2.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	89.090, 144.120, 158.740, 90.00, 90.00, 90.00
R / Rfree (%)	22.6 / 25.8

The structure of Crystal Structure of the Metalloproteinase Enhancer Pcpe-1 Bound to the Procollagen C Propeptide Trimer (Short) also contains other interesting chemical elements:

Calcium

(Ca)

5 atoms

The binding sites of Chlorine atom in the Crystal Structure of the Metalloproteinase Enhancer Pcpe-1 Bound to the Procollagen C Propeptide Trimer (Short) (pdb code 6fzv). 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 the Metalloproteinase Enhancer Pcpe-1 Bound to the Procollagen C Propeptide Trimer (Short), PDB code: 6fzv:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of the Metalloproteinase Enhancer Pcpe-1 Bound to the Procollagen C Propeptide Trimer (Short)


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 the Metalloproteinase Enhancer Pcpe-1 Bound to the Procollagen C Propeptide Trimer (Short) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl303 b:89.5 occ:1.00 HH12 B:ARG42 2.7 0.0 1.0 HH22 B:ARG42 2.8 0.2 1.0 HE3 B:LYS45 3.1 71.4 1.0 HA B:PHE46 3.4 81.3 1.0 NH1 B:ARG42 3.5 86.7 1.0 NH2 B:ARG42 3.5 86.0 1.0 HG2 B:LYS45 3.5 71.5 1.0 HD2 B:PHE46 3.7 89.8 1.0 CD2 B:PHE46 3.7 74.8 1.0 CE2 B:PHE46 3.9 74.3 1.0 CZ B:ARG42 4.0 86.0 1.0 HE2 B:PHE46 4.0 89.1 1.0 CE B:LYS45 4.0 59.5 1.0 HH11 B:ARG42 4.2 0.0 1.0 CG B:PHE46 4.2 74.5 1.0 HH21 B:ARG42 4.2 0.2 1.0 CA B:PHE46 4.3 67.7 1.0 CG B:LYS45 4.4 59.6 1.0 HE2 B:LYS45 4.4 71.4 1.0 CZ B:PHE46 4.5 73.6 1.0 HD3 B:LYS45 4.5 99.3 1.0 CD B:LYS45 4.6 82.8 1.0 O B:LYS45 4.6 60.1 1.0 CB B:PHE46 4.7 72.1 1.0 N B:PHE46 4.7 67.8 1.0 HZ1 B:LYS45 4.8 0.1 1.0 CD1 B:PHE46 4.8 74.8 1.0 HG2 A:PRO125 4.8 72.8 1.0 C B:LYS45 4.8 59.9 1.0 HZ3 B:LYS45 4.8 0.1 1.0 NZ B:LYS45 4.8 87.6 1.0 HB2 B:PHE46 4.9 86.5 1.0 HG3 B:LYS45 4.9 71.5 1.0 CE1 B:PHE46 4.9 74.4 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of the Metalloproteinase Enhancer Pcpe-1 Bound to the Procollagen C Propeptide Trimer (Short)


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 the Metalloproteinase Enhancer Pcpe-1 Bound to the Procollagen C Propeptide Trimer (Short) within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl303 b:99.8 occ:1.00 HH22 C:ARG42 2.4 0.9 1.0 HH12 C:ARG42 2.7 77.3 1.0 NH2 C:ARG42 3.2 85.0 1.0 HE3 C:LYS45 3.4 79.8 1.0 NH1 C:ARG42 3.4 64.4 1.0 CZ C:ARG42 3.7 84.9 1.0 HH21 C:ARG42 3.8 0.9 1.0 HA C:PHE46 3.9 95.8 1.0 CE2 C:PHE46 3.9 76.8 1.0 HG2 C:LYS45 4.0 79.6 1.0 CD2 C:PHE46 4.0 77.3 1.0 HE2 C:PHE46 4.1 92.2 1.0 HH11 C:ARG42 4.1 77.3 1.0 HD2 C:PHE46 4.2 92.8 1.0 CZ C:PHE46 4.2 75.8 1.0 CG C:PHE46 4.3 77.6 1.0 CE C:LYS45 4.3 66.5 1.0 HG2 B:PRO125 4.5 79.3 1.0 CE1 C:PHE46 4.5 76.1 1.0 CD1 C:PHE46 4.5 76.6 1.0 HZ C:PHE46 4.6 91.0 1.0 HE2 C:LYS45 4.6 79.8 1.0 CA C:PHE46 4.8 79.9 1.0 CG C:LYS45 4.8 66.3 1.0 HD3 C:LYS45 4.9 79.4 1.0 CD C:LYS45 4.9 66.2 1.0 O C:LYS45 5.0 87.3 1.0

D.Pulido, U.Sharma, S.Vadon-Le Goff, S.A.Hussain, S.Cordes, N.Mariano, E.Bettler, C.Moali, N.Aghajari, E.Hohenester, D.J.S.Hulmes. Structural Basis For the Acceleration of Procollagen Processing By Procollagen C-Proteinase Enhancer-1. Structure V. 26 1384 2018.
ISSN: ISSN 1878-4186
PubMed: 30078642
DOI: 10.1016/J.STR.2018.06.011