Chlorine in PDB 3bic: Crystal Structure of Human Methylmalonyl-Coa Mutase

All present enzymatic activity of Crystal Structure of Human Methylmalonyl-Coa Mutase:
5.4.99.2;

The structure of Crystal Structure of Human Methylmalonyl-Coa Mutase, PDB code: 3bic was solved by E.Ugochukwu, G.Kochan, N.Pantic, E.Parizotto, E.S.Pilka, A.C.W.Pike, O.Gileadi, F.Von Delft, C.H.Arrowsmith, J.Weigelt, A.M.Edwards, U.Oppermann, Structural Genomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.42 / 2.60
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	103.750, 95.150, 119.160, 90.00, 108.31, 90.00
R / Rfree (%)	21.7 / 24.3

The binding sites of Chlorine atom in the Crystal Structure of Human Methylmalonyl-Coa Mutase (pdb code 3bic). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Crystal Structure of Human Methylmalonyl-Coa Mutase, PDB code: 3bic:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Crystal Structure of Human Methylmalonyl-Coa Mutase


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 Human Methylmalonyl-Coa Mutase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl801 b:45.7 occ:1.00 O A:HOH918 4.1 27.3 1.0 NE2 A:HIS627 4.1 43.9 1.0 CD2 A:HIS265 4.3 38.4 1.0 CE2 A:TYR264 4.4 37.0 1.0 O A:HOH921 4.5 44.5 1.0 NE A:ARG228 4.6 53.6 1.0 NE2 A:HIS265 4.7 39.2 1.0 CD A:ARG228 4.7 51.9 1.0 O A:HOH920 4.8 31.1 1.0 CE1 A:HIS627 4.8 43.1 1.0

Chlorine binding site 2 out of 4 in the Crystal Structure of Human Methylmalonyl-Coa Mutase


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 Human Methylmalonyl-Coa Mutase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl803 b:78.0 occ:1.00 N A:LYS595 3.3 45.0 1.0 OG A:SER594 3.7 45.9 1.0 CB A:LYS595 4.0 44.7 1.0 CA A:SER594 4.0 45.5 1.0 N A:GLU596 4.1 44.7 1.0 CA A:LYS595 4.1 44.9 1.0 C A:SER594 4.2 45.2 1.0 CB A:SER594 4.2 45.5 1.0 C A:LYS595 4.7 44.9 1.0 CB A:GLU596 4.9 44.6 1.0

Chlorine binding site 3 out of 4 in the Crystal Structure of Human Methylmalonyl-Coa Mutase


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 Human Methylmalonyl-Coa Mutase within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl802 b:41.7 occ:1.00 NE2 B:HIS627 3.9 46.8 1.0 CD2 B:HIS265 4.0 38.7 1.0 CD B:ARG228 4.1 48.6 1.0 CE2 B:TYR264 4.4 36.7 1.0 NE2 B:HIS265 4.4 40.4 1.0 NH2 B:ARG228 4.6 53.8 1.0 CE1 B:HIS627 4.7 46.2 1.0 CD2 B:HIS627 4.9 45.4 1.0 NE B:ARG228 5.0 51.8 1.0 CG B:ARG228 5.0 46.6 1.0

Chlorine binding site 4 out of 4 in the Crystal Structure of Human Methylmalonyl-Coa Mutase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of Human Methylmalonyl-Coa Mutase within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl804 b:61.5 occ:1.00 CA B:GLY670 4.0 43.4 1.0 CG2 B:ILE634 4.3 36.2 1.0 CD1 B:PHE722 4.4 49.0 1.0 CB B:MET700 4.5 44.2 1.0 C B:GLY670 4.5 44.4 1.0 O B:MET700 4.7 45.4 1.0 N B:VAL671 4.8 45.5 1.0 CE1 B:PHE722 4.9 48.7 1.0 C B:MET700 4.9 45.2 1.0 O B:VAL671 5.0 47.4 1.0

D.S.Froese, G.Kochan, J.R.Muniz, X.Wu, C.Gileadi, E.Ugochukwu, E.Krysztofinska, R.A.Gravel, U.Oppermann, W.W.Yue. Structures of the Human Gtpase Mmaa and Vitamin B12-Dependent Methylmalonyl-Coa Mutase and Insight Into Their Complex Formation. J.Biol.Chem. V. 285 38204 2010.
ISSN: ISSN 0021-9258
PubMed: 20876572
DOI: 10.1074/JBC.M110.177717