Chlorine in PDB 3cqo: Crystal Structure of A F-Lectin (Fucolectin) From Morone Saxatilis (Striped Bass) Serum

The structure of Crystal Structure of A F-Lectin (Fucolectin) From Morone Saxatilis (Striped Bass) Serum, PDB code: 3cqo was solved by M.A.Bianchet, L.M.Amzel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.15 / 2.32
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	88.135, 88.135, 230.169, 90.00, 90.00, 90.00
R / Rfree (%)	18.4 / 24.5

The structure of Crystal Structure of A F-Lectin (Fucolectin) From Morone Saxatilis (Striped Bass) Serum also contains other interesting chemical elements:

Calcium

(Ca)

6 atoms

The binding sites of Chlorine atom in the Crystal Structure of A F-Lectin (Fucolectin) From Morone Saxatilis (Striped Bass) Serum (pdb code 3cqo). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of A F-Lectin (Fucolectin) From Morone Saxatilis (Striped Bass) Serum, PDB code: 3cqo:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of A F-Lectin (Fucolectin) From Morone Saxatilis (Striped Bass) Serum


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 A F-Lectin (Fucolectin) From Morone Saxatilis (Striped Bass) Serum within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl5001 b:18.4 occ:1.00 O C:HOH4118 3.1 31.5 1.0 O A:HOH5084 3.6 33.3 1.0 NH1 C:ARG17 3.6 23.5 1.0 O C:HOH4075 3.6 34.5 1.0 NH1 A:ARG17 3.8 16.4 1.0 NH1 B:ARG17 3.8 16.7 1.0 NH2 C:ARG17 3.9 21.2 1.0 NH2 B:ARG17 3.9 18.5 1.0 O A:HOH5008 4.0 12.8 1.0 NH2 A:ARG17 4.0 12.8 1.0 CZ C:ARG17 4.2 21.6 1.0 CB C:ALA24 4.2 19.9 1.0 CB B:ALA24 4.2 15.7 1.0 O B:HOH4015 4.2 23.2 1.0 O C:HOH4007 4.2 13.7 1.0 CB A:ALA24 4.3 15.8 1.0 CZ B:ARG17 4.3 19.2 1.0 CZ A:ARG17 4.4 16.8 1.0 O A:THR21 4.6 21.6 1.0 O C:THR21 4.7 22.2 1.0 O B:THR21 4.7 24.7 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of A F-Lectin (Fucolectin) From Morone Saxatilis (Striped Bass) Serum


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 A F-Lectin (Fucolectin) From Morone Saxatilis (Striped Bass) Serum within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl5002 b:25.3 occ:1.00 NZ B:LYS11 3.3 19.8 1.0 NZ A:LYS11 3.4 15.3 1.0 NZ C:LYS11 3.5 21.0 1.0 CE B:LYS11 3.8 17.8 1.0 CE C:LYS11 3.9 22.0 1.0 CE A:LYS11 4.0 15.2 1.0 CD C:LYS11 4.2 19.1 1.0 CD B:LYS11 4.2 17.0 1.0 CE1 C:TYR26 4.2 20.0 1.0 CE1 A:TYR26 4.3 21.8 1.0 CD A:LYS11 4.3 15.3 1.0 CE1 B:TYR26 4.4 21.6 1.0 O A:GLY10 4.4 15.8 1.0 O B:HOH4073 4.5 23.7 1.0 O C:GLY10 4.6 18.3 1.0 O B:GLY10 4.7 20.4 1.0 O C:HOH4130 4.7 36.0 1.0 CD1 A:TYR26 4.8 21.9 1.0 CD1 C:TYR26 4.8 19.1 1.0 CD1 B:TYR26 5.0 21.9 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of A F-Lectin (Fucolectin) From Morone Saxatilis (Striped Bass) Serum


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of A F-Lectin (Fucolectin) From Morone Saxatilis (Striped Bass) Serum within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl5003 b:22.8 occ:1.00 O C:HOH4128 2.9 45.2 1.0 NZ B:LYS159 3.2 26.9 1.0 NZ A:LYS159 3.5 23.7 1.0 NZ C:LYS159 3.6 21.8 1.0 O A:HOH5069 3.7 25.2 1.0 CE B:LYS159 3.9 27.0 1.0 CE C:LYS159 4.0 18.8 1.0 CE1 A:TYR172 4.0 20.9 1.0 CE1 B:TYR172 4.0 21.9 1.0 CE A:LYS159 4.1 23.1 1.0 CE1 C:TYR172 4.2 27.1 1.0 CD C:LYS159 4.3 20.0 1.0 CD A:LYS159 4.4 22.9 1.0 CD B:LYS159 4.5 28.4 1.0 O C:GLY158 4.5 20.4 1.0 CD1 A:TYR172 4.5 21.8 1.0 O A:GLY158 4.6 27.0 1.0 O B:GLY158 4.7 27.9 1.0 CD1 B:TYR172 4.8 23.6 1.0 CD1 C:TYR172 4.8 26.9 1.0 OH B:TYR172 4.9 23.2 1.0 CZ B:TYR172 5.0 21.8 1.0

M.A.Bianchet, E.W.Odom, G.R.Vasta, L.M.Amzel. Structure and Specificity of A Binary Tandem Domain F-Lectin From Striped Bass (Morone Saxatilis). J.Mol.Biol. V. 401 239 2010.
ISSN: ISSN 0022-2836
PubMed: 20561530
DOI: 10.1016/J.JMB.2010.06.018