Chlorine in PDB 2v3p: Crystallographic Analysis of Beta-Axial Ligand Substitutions in Cobalamin Bound to Transcobalamin

The structure of Crystallographic Analysis of Beta-Axial Ligand Substitutions in Cobalamin Bound to Transcobalamin, PDB code: 2v3p was solved by J.Wuerges, S.Geremia, L.Randaccio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.98 / 2.90
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	100.390, 100.390, 129.742, 90.00, 90.00, 120.00
R / Rfree (%)	19.4 / 25

The structure of Crystallographic Analysis of Beta-Axial Ligand Substitutions in Cobalamin Bound to Transcobalamin also contains other interesting chemical elements:

Cobalt

(Co)

1 atom

The binding sites of Chlorine atom in the Crystallographic Analysis of Beta-Axial Ligand Substitutions in Cobalamin Bound to Transcobalamin (pdb code 2v3p). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystallographic Analysis of Beta-Axial Ligand Substitutions in Cobalamin Bound to Transcobalamin, PDB code: 2v3p:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystallographic Analysis of Beta-Axial Ligand Substitutions in Cobalamin Bound to Transcobalamin


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystallographic Analysis of Beta-Axial Ligand Substitutions in Cobalamin Bound to Transcobalamin within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1416 b:43.4 occ:1.00 N A:GLN269 3.0 42.5 1.0 N A:ASN270 3.0 41.1 1.0 NE2 A:GLN394 3.2 28.7 1.0 OH A:TYR229 3.4 36.2 1.0 N33 A:B121415 3.5 31.4 1.0 CB A:ASN270 3.5 40.8 1.0 O A:THR267 3.6 46.6 1.0 CA A:GLN269 3.7 41.9 1.0 CB A:GLN269 3.7 42.0 1.0 CE1 A:TYR229 3.7 34.2 1.0 C A:GLN269 3.8 41.6 1.0 CZ A:TYR229 3.8 35.1 1.0 CA A:ASN270 3.9 40.6 1.0 C A:PHE268 4.0 43.5 1.0 CA A:PHE268 4.1 43.8 1.0 CG A:GLN394 4.1 30.0 1.0 CD A:GLN394 4.2 29.0 1.0 CG A:GLN269 4.4 43.9 1.0 CB A:ASP398 4.4 39.8 1.0 O A:HOH2116 4.5 42.9 1.0 C32 A:B121415 4.5 32.2 1.0 CG A:ASP398 4.6 40.7 1.0 C A:THR267 4.6 46.9 1.0 OD2 A:ASP398 4.7 41.6 1.0 O34 A:B121415 4.7 33.4 1.0 CG A:MET273 4.7 38.4 1.0 CB A:MET273 4.8 38.1 1.0 CD1 A:TYR229 4.8 35.4 1.0 N A:PHE268 4.9 45.2 1.0 CG A:ASN270 4.9 41.3 1.0 CE2 A:TYR229 4.9 33.7 1.0 O A:GLN269 5.0 41.7 1.0

Chlorine binding site 2 out of 3 in the Crystallographic Analysis of Beta-Axial Ligand Substitutions in Cobalamin Bound to Transcobalamin


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystallographic Analysis of Beta-Axial Ligand Substitutions in Cobalamin Bound to Transcobalamin within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1417 b:41.6 occ:1.00 OG A:SER370 3.1 33.7 1.0 N A:GLY373 3.3 34.8 1.0 NH1 A:ARG356 3.4 56.8 1.0 NE A:ARG358 3.5 53.4 1.0 CA A:PHE357 3.5 40.8 1.0 C A:PHE357 3.7 41.2 1.0 N A:PHE357 3.7 41.2 1.0 CB A:SER370 3.8 33.8 1.0 CZ A:ARG356 3.8 57.1 1.0 CA A:GLY373 3.8 35.4 1.0 N A:ARG358 3.9 40.8 1.0 N A:LEU372 3.9 33.7 1.0 CG A:ARG358 3.9 43.0 1.0 C A:ARG356 4.0 41.7 1.0 CG A:ARG356 4.0 45.5 1.0 C A:SER370 4.0 33.5 1.0 O A:ARG356 4.0 41.3 1.0 N A:VAL371 4.0 33.7 1.0 O A:SER370 4.1 33.6 1.0 C A:VAL371 4.1 33.5 1.0 O A:PHE357 4.2 41.6 1.0 CA A:VAL371 4.2 33.4 1.0 CD A:ARG358 4.3 48.9 1.0 NH2 A:ARG356 4.3 57.5 1.0 NH2 A:ARG358 4.3 55.1 1.0 CB A:ARG358 4.3 40.8 1.0 C A:LEU372 4.3 34.3 1.0 CZ A:ARG358 4.4 55.1 1.0 NE A:ARG356 4.4 55.8 1.0 CA A:LEU372 4.5 33.9 1.0 O A:HOH2085 4.5 53.5 1.0 CA A:SER370 4.6 33.6 1.0 C A:GLY373 4.7 36.0 1.0 CB A:ARG356 4.7 42.9 1.0 CD A:ARG356 4.7 51.6 1.0 CA A:ARG358 4.7 40.7 1.0 O A:VAL371 4.8 33.3 1.0 N A:ARG374 4.9 36.4 1.0 CB A:PHE357 4.9 40.2 1.0 CA A:ARG356 5.0 42.4 1.0

Chlorine binding site 3 out of 3 in the Crystallographic Analysis of Beta-Axial Ligand Substitutions in Cobalamin Bound to Transcobalamin


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystallographic Analysis of Beta-Axial Ligand Substitutions in Cobalamin Bound to Transcobalamin within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1418 b:77.6 occ:1.00 NH2 A:ARG108 3.1 40.6 1.0 NE A:ARG108 3.2 42.1 1.0 NE2 A:GLN112 3.4 39.8 1.0 O A:HOH2030 3.6 60.9 1.0 CZ A:ARG108 3.6 41.5 1.0 CG A:GLN112 3.9 35.9 1.0 O A:ARG108 4.0 40.2 1.0 CD A:GLN112 4.1 38.2 1.0 CB A:ARG108 4.2 39.7 1.0 CD A:ARG108 4.4 40.1 1.0 CG A:ARG108 4.4 39.6 1.0 C A:ARG108 4.6 39.8 1.0 CA A:ARG108 4.6 39.9 1.0 NH1 A:ARG115 4.8 54.0 1.0 CD2 A:LEU67 4.8 66.5 1.0 NH1 A:ARG108 4.9 40.2 1.0

J.Wuerges, S.Geremia, S.N.Fedosov, L.Randaccio. Vitamin B12 Transport Proteins: Crystallographic Analysis of Beta-Axial Ligand Substitutions in Cobalamin Bound to Transcobalamin. Iubmb Life V. 59 722 2007.
ISSN: ISSN 1521-6543
PubMed: 17943552
DOI: 10.1080/15216540701673413