Chlorine in PDB 1w7v: Znmg Substituted Aminopeptidase P From E. Coli

All present enzymatic activity of Znmg Substituted Aminopeptidase P From E. Coli:
3.4.11.9;

The structure of Znmg Substituted Aminopeptidase P From E. Coli, PDB code: 1w7v was solved by S.C.Graham, C.S.Bond, H.C.Freeman, J.M.Guss, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.80 / 2.00
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	111.731, 236.527, 137.997, 90.00, 106.34, 90.00
R / Rfree (%)	15.6 / 18

The structure of Znmg Substituted Aminopeptidase P From E. Coli also contains other interesting chemical elements:

Magnesium	(Mg)	6 atoms
Zinc	(Zn)	4 atoms

The binding sites of Chlorine atom in the Znmg Substituted Aminopeptidase P From E. Coli (pdb code 1w7v). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Znmg Substituted Aminopeptidase P From E. Coli, PDB code: 1w7v:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Znmg Substituted Aminopeptidase P From E. Coli


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Znmg Substituted Aminopeptidase P From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1442 b:47.7 occ:1.00 O A:HOH2081 3.2 52.5 1.0 N A:VAL80 3.3 38.7 1.0 N A:SER111 3.4 36.7 1.0 CB A:SER111 3.7 39.9 1.0 CA A:ARG79 3.7 38.6 1.0 OG A:SER111 3.8 44.3 1.0 N A:PHE110 3.8 33.8 1.0 CG1 A:VAL80 3.8 43.0 1.0 CB A:VAL80 4.0 44.3 1.0 C A:ARG79 4.0 35.7 1.0 CA A:SER111 4.1 39.2 1.0 O A:ASN78 4.2 32.5 1.0 CB A:PHE110 4.2 35.0 1.0 CB A:ALA109 4.2 36.8 1.0 C A:PHE110 4.3 36.1 1.0 CA A:PHE110 4.3 34.7 1.0 CA A:VAL80 4.3 43.1 1.0 C A:ALA109 4.4 35.9 1.0 CB A:ARG79 4.4 40.3 1.0 CA A:ALA109 4.6 36.8 1.0 CG A:ARG79 4.6 42.6 0.6 CG A:ARG79 4.6 43.3 0.4 N A:ARG79 4.7 33.5 1.0 C A:ASN78 4.8 33.3 1.0

Chlorine binding site 2 out of 4 in the Znmg Substituted Aminopeptidase P From E. Coli


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Znmg Substituted Aminopeptidase P From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1443 b:40.0 occ:1.00 N B:SER111 3.3 36.5 1.0 N B:VAL80 3.4 38.8 1.0 CB B:SER111 3.6 40.6 1.0 N B:PHE110 3.8 33.8 1.0 OG B:SER111 3.8 45.6 1.0 CA B:ARG79 3.8 38.7 1.0 CG1 B:VAL80 3.8 43.0 1.0 CB B:VAL80 4.0 43.9 1.0 CA B:SER111 4.1 39.1 1.0 C B:ARG79 4.1 35.6 1.0 CB B:PHE110 4.2 35.9 1.0 O B:ASN78 4.2 32.7 1.0 CB B:ALA109 4.2 36.6 1.0 C B:PHE110 4.2 36.1 1.0 CA B:PHE110 4.3 34.8 1.0 CA B:VAL80 4.3 43.0 1.0 C B:ALA109 4.4 35.9 1.0 CB B:ARG79 4.5 40.7 1.0 CA B:ALA109 4.6 36.7 1.0 CG B:ARG79 4.7 42.9 0.6 CG B:ARG79 4.8 43.5 0.4 N B:ARG79 4.8 33.2 1.0 C B:ASN78 4.9 33.2 1.0

Chlorine binding site 3 out of 4 in the Znmg Substituted Aminopeptidase P From E. Coli


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Znmg Substituted Aminopeptidase P From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl1442 b:54.0 occ:1.00 N C:VAL80 3.4 38.7 1.0 N C:SER111 3.4 36.4 1.0 CB C:SER111 3.6 40.1 1.0 CG1 C:VAL80 3.7 43.9 1.0 OG C:SER111 3.7 44.0 1.0 N C:PHE110 3.8 33.9 1.0 CA C:ARG79 3.8 38.7 1.0 CB C:VAL80 3.9 44.4 1.0 CA C:SER111 4.1 39.2 1.0 C C:ARG79 4.1 35.6 1.0 CB C:ALA109 4.1 35.8 1.0 O C:ASN78 4.2 32.6 1.0 CB C:PHE110 4.3 36.5 1.0 CA C:VAL80 4.3 43.1 1.0 C C:PHE110 4.3 36.2 1.0 CA C:PHE110 4.3 34.8 1.0 C C:ALA109 4.4 35.8 1.0 CA C:ALA109 4.5 36.8 1.0 CB C:ARG79 4.6 39.8 1.0 CG C:ARG79 4.8 42.0 0.6 N C:ARG79 4.8 33.3 1.0 CG C:ARG79 4.8 42.9 0.4 C C:ASN78 4.9 33.3 1.0

Chlorine binding site 4 out of 4 in the Znmg Substituted Aminopeptidase P From E. Coli


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Znmg Substituted Aminopeptidase P From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl1443 b:45.8 occ:1.00 N D:SER111 3.3 36.8 1.0 N D:VAL80 3.4 38.7 1.0 CB D:SER111 3.6 39.6 1.0 OG D:SER111 3.8 44.9 1.0 N D:PHE110 3.8 33.7 1.0 CA D:ARG79 3.8 38.5 1.0 CG1 D:VAL80 3.8 44.7 1.0 CB D:VAL80 4.0 43.8 1.0 CA D:SER111 4.1 39.3 1.0 C D:ARG79 4.1 35.7 1.0 CB D:PHE110 4.2 37.2 1.0 CB D:ALA109 4.2 36.5 1.0 C D:PHE110 4.2 36.0 1.0 O D:ASN78 4.2 32.4 1.0 CA D:PHE110 4.3 34.7 1.0 CA D:VAL80 4.3 43.2 1.0 C D:ALA109 4.4 35.9 1.0 CB D:ARG79 4.5 41.2 1.0 CA D:ALA109 4.6 36.9 1.0 CG D:ARG79 4.6 42.5 0.6 CG D:ARG79 4.7 43.2 0.4 N D:ARG79 4.8 33.3 1.0 C D:ASN78 4.9 33.2 1.0

S.C.Graham, C.S.Bond, H.C.Freeman, J.M.Guss. Structural and Functional Implications of Metal Ion Selection in Aminopeptidase P, A Metalloprotease with A Dinuclear Metal Center. Biochemistry V. 44 13820 2005.
ISSN: ISSN 0006-2960
PubMed: 16229471
DOI: 10.1021/BI0512849