Chlorine in PDB 4akd: High Resolution Structure of Mannose Binding Lectin From Champedak (Cmb)

The structure of High Resolution Structure of Mannose Binding Lectin From Champedak (Cmb), PDB code: 4akd was solved by M.Gabrielsen, P.S.Abdul-Rahman, S.Othman, O.H.Hashim, R.J.Cogdell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.69 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	76.887, 86.222, 95.373, 90.00, 90.00, 90.00
R / Rfree (%)	19.34 / 23.57

The structure of High Resolution Structure of Mannose Binding Lectin From Champedak (Cmb) also contains other interesting chemical elements:

Cadmium

(Cd)

8 atoms

The binding sites of Chlorine atom in the High Resolution Structure of Mannose Binding Lectin From Champedak (Cmb) (pdb code 4akd). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 7 binding sites of Chlorine where determined in the High Resolution Structure of Mannose Binding Lectin From Champedak (Cmb), PDB code: 4akd:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6; 7;

Chlorine binding site 1 out of 7 in the High Resolution Structure of Mannose Binding Lectin From Champedak (Cmb)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of High Resolution Structure of Mannose Binding Lectin From Champedak (Cmb) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1154 b:95.9 occ:1.00 OE2 B:GLU117 1.9 90.4 0.0 CD B:GLU117 2.8 94.1 0.0 CG B:GLU117 3.0 71.3 0.0 CD B:CD1152 3.3 69.0 1.0 CD B:CD1151 3.5 63.5 1.0 OE1 B:GLU117 3.9 88.1 0.0 OD1 B:ASP115 4.3 74.6 1.0 CL B:CL1155 4.4 61.2 1.0 CL B:CL1157 4.4 60.0 1.0 CB B:GLU117 4.5 58.4 1.0

Chlorine binding site 2 out of 7 in the High Resolution Structure of Mannose Binding Lectin From Champedak (Cmb)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of High Resolution Structure of Mannose Binding Lectin From Champedak (Cmb) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1155 b:61.2 occ:1.00 CD B:CD1152 2.8 69.0 1.0 CD B:CD1151 2.8 63.5 1.0 OE2 B:GLU36 2.8 92.5 0.0 OD2 B:ASP115 3.3 84.6 1.0 OD1 B:ASP115 3.5 74.6 1.0 OE2 B:GLU117 3.6 90.4 0.0 CG B:ASP115 3.8 74.2 1.0 CD B:GLU36 4.0 98.1 0.0 CL B:CL1157 4.0 60.0 1.0 CL B:CL1154 4.4 95.9 1.0 OE1 B:GLU36 4.5 93.7 0.0 CD B:GLU117 4.6 94.1 0.0

Chlorine binding site 3 out of 7 in the High Resolution Structure of Mannose Binding Lectin From Champedak (Cmb)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of High Resolution Structure of Mannose Binding Lectin From Champedak (Cmb) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1156 b:65.8 occ:1.00 CD B:CD1153 2.6 0.9 1.0 CD B:CD1151 3.0 63.5 1.0 OG B:SER88 3.3 87.3 1.0 OE1 B:GLU117 3.5 88.1 0.0 NH2 B:ARG98 3.9 50.3 1.0 OE2 B:GLU36 4.0 92.5 0.0 CG B:GLU36 4.3 75.4 0.0 CB B:SER88 4.3 78.7 1.0 CD B:GLU117 4.4 94.1 0.0 OE2 B:GLU117 4.4 90.4 0.0 CD B:GLU36 4.5 98.1 0.0 CE1 B:PHE87 4.6 70.9 1.0 NH1 B:ARG98 4.7 49.5 1.0 CZ B:ARG98 4.7 59.6 1.0 CD1 B:PHE87 4.7 67.3 1.0

Chlorine binding site 4 out of 7 in the High Resolution Structure of Mannose Binding Lectin From Champedak (Cmb)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of High Resolution Structure of Mannose Binding Lectin From Champedak (Cmb) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1157 b:60.0 occ:1.00 CD B:CD1152 2.5 69.0 1.0 CL B:CL1155 4.0 61.2 1.0 CL B:CL1154 4.4 95.9 1.0

Chlorine binding site 5 out of 7 in the High Resolution Structure of Mannose Binding Lectin From Champedak (Cmb)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of High Resolution Structure of Mannose Binding Lectin From Champedak (Cmb) within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl1153 b:0.2 occ:1.00 OE2 C:GLU117 2.6 0.5 0.0 CD C:CD1152 2.9 94.4 1.0 CD C:GLU117 3.8 0.7 0.0 O C:GLU116 4.1 1.0 1.0 OD1 C:ASP115 4.3 0.4 1.0 OE1 C:GLU117 4.6 0.3 0.0 CG C:GLU117 4.6 0.4 0.0

Chlorine binding site 6 out of 7 in the High Resolution Structure of Mannose Binding Lectin From Champedak (Cmb)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of High Resolution Structure of Mannose Binding Lectin From Champedak (Cmb) within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl1154 b:74.5 occ:1.00 CD C:CD1151 2.8 91.4 1.0 CD C:CD1152 2.9 94.4 1.0 O C:HOH2040 3.1 62.0 1.0 OD2 C:ASP115 3.4 0.9 1.0 OE1 C:GLU117 3.8 0.3 0.0 CL C:CL1155 3.9 34.4 1.0 CG C:ASP115 4.2 0.6 1.0 OD1 C:ASP115 4.4 0.4 1.0 CD C:GLU117 4.6 0.7 0.0 O C:HOH2041 4.6 54.7 1.0 OE2 C:GLU117 4.7 0.5 0.0

Chlorine binding site 7 out of 7 in the High Resolution Structure of Mannose Binding Lectin From Champedak (Cmb)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 7 of High Resolution Structure of Mannose Binding Lectin From Champedak (Cmb) within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl1155 b:34.4 occ:1.00 CD C:CD1151 1.6 91.4 1.0 OE1 C:GLU117 3.1 0.3 0.0 CD C:CD2000 3.2 82.7 1.0 CL C:CL1154 3.9 74.5 1.0 CD C:GLU117 4.1 0.7 0.0 CG C:GLU117 4.5 0.4 0.0 CD C:CD1152 4.6 94.4 1.0 O C:HOH2040 4.7 62.0 1.0 CB C:GLU117 4.9 1.0 0.0

M.Gabrielsen, P.S.Abdul-Rahman, S.Othman, O.H.Hashim, R.J.Cogdell. Structures and Binding Specificity of Galactose- and Mannose-Binding Lectins From Champedak: Differences From Jackfruit Lectins Acta Crystallogr.,Sect.F V. 70 709 2014.
ISSN: ISSN 1744-3091
PubMed: 24915077
DOI: 10.1107/S2053230X14008966