Chlorine in PDB 1wbq: 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: 1wbq 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)	29.97 / 2.30
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	111.974, 236.703, 137.637, 90.00, 106.14, 90.00
R / Rfree (%)	16.7 / 19.7

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 1wbq). 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: 1wbq:
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:49.1 occ:1.00 N A:VAL80 3.3 41.4 1.0 N A:SER111 3.4 35.4 1.0 CA A:ARG79 3.6 43.0 1.0 N A:PHE110 3.7 33.8 1.0 CB A:SER111 3.8 36.3 1.0 OG A:SER111 3.8 41.9 1.0 CG1 A:VAL80 4.0 40.2 1.0 C A:ARG79 4.0 40.9 1.0 CB A:PHE110 4.1 35.6 1.0 CB A:VAL80 4.1 44.8 1.0 O A:ASN78 4.2 35.4 1.0 CA A:SER111 4.2 38.5 1.0 CA A:PHE110 4.2 35.5 1.0 CB A:ARG79 4.2 42.2 1.0 C A:PHE110 4.2 36.0 1.0 CB A:ALA109 4.3 32.6 1.0 CG A:ARG79 4.3 49.8 1.0 CA A:VAL80 4.3 44.7 1.0 C A:ALA109 4.4 33.9 1.0 CA A:ALA109 4.6 36.5 1.0 N A:ARG79 4.6 40.7 1.0 C A:ASN78 4.8 37.5 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:38.6 occ:1.00 N B:VAL80 3.4 41.3 1.0 N B:SER111 3.4 35.4 1.0 CA B:ARG79 3.7 43.0 1.0 N B:PHE110 3.7 34.0 1.0 CB B:SER111 3.7 35.6 1.0 OG B:SER111 3.8 40.7 1.0 CG1 B:VAL80 4.0 39.8 1.0 C B:ARG79 4.1 40.8 1.0 CB B:PHE110 4.1 36.4 1.0 CA B:SER111 4.1 38.5 1.0 CB B:VAL80 4.2 44.1 1.0 CA B:PHE110 4.2 35.6 1.0 O B:ASN78 4.2 35.4 1.0 C B:PHE110 4.2 36.2 1.0 CB B:ALA109 4.3 34.6 1.0 CB B:ARG79 4.3 41.6 1.0 CA B:VAL80 4.4 44.8 1.0 C B:ALA109 4.4 33.9 1.0 CG B:ARG79 4.4 50.2 1.0 CA B:ALA109 4.6 36.5 1.0 N B:ARG79 4.7 40.7 1.0 C B:ASN78 4.8 37.5 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:49.0 occ:1.00 N C:SER111 3.3 35.3 1.0 N C:VAL80 3.4 41.4 1.0 N C:PHE110 3.6 33.9 1.0 CB C:SER111 3.7 37.0 1.0 CA C:ARG79 3.7 43.0 1.0 OG C:SER111 3.7 41.8 1.0 CG1 C:VAL80 4.0 40.0 1.0 CB C:PHE110 4.1 36.3 1.0 CA C:SER111 4.1 38.4 1.0 C C:ARG79 4.1 40.9 1.0 CA C:PHE110 4.1 35.6 1.0 C C:PHE110 4.2 36.2 1.0 CB C:VAL80 4.2 44.8 1.0 O C:ASN78 4.2 35.5 1.0 CB C:ALA109 4.2 33.6 1.0 C C:ALA109 4.3 33.9 1.0 CB C:ARG79 4.4 41.5 1.0 CA C:VAL80 4.4 44.8 1.0 CA C:ALA109 4.5 36.4 1.0 CG C:ARG79 4.6 49.1 1.0 N C:ARG79 4.7 40.7 1.0 C C:ASN78 4.8 37.6 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:45.7 occ:1.00 N D:SER111 3.4 35.4 1.0 N D:VAL80 3.4 41.4 1.0 CB D:SER111 3.7 35.0 1.0 CA D:ARG79 3.7 43.0 1.0 N D:PHE110 3.7 34.0 1.0 OG D:SER111 3.8 40.7 1.0 CG1 D:VAL80 3.9 39.3 1.0 C D:ARG79 4.1 40.8 1.0 CB D:VAL80 4.1 44.2 1.0 CA D:SER111 4.1 38.5 1.0 CB D:PHE110 4.2 36.8 1.0 CA D:PHE110 4.2 35.5 1.0 C D:PHE110 4.2 36.0 1.0 CB D:ALA109 4.2 33.7 1.0 O D:ASN78 4.3 35.5 1.0 CB D:ARG79 4.3 42.0 1.0 CA D:VAL80 4.4 44.8 1.0 C D:ALA109 4.4 33.9 1.0 CG D:ARG79 4.4 48.5 1.0 CA D:ALA109 4.6 36.5 1.0 N D:ARG79 4.7 40.6 1.0 C D:ASN78 4.8 37.5 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