Chlorine in PDB 3oxo: Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart Covalently Bound to Coa

All present enzymatic activity of Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart Covalently Bound to Coa:
2.8.3.5;

The structure of Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart Covalently Bound to Coa, PDB code: 3oxo was solved by M.E.Fraser, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	21.20 / 2.30
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	69.121, 107.133, 134.565, 89.60, 80.21, 75.13
R / Rfree (%)	24.5 / 27.3

The binding sites of Chlorine atom in the Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart Covalently Bound to Coa (pdb code 3oxo). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart Covalently Bound to Coa, PDB code: 3oxo:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart Covalently Bound to Coa


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart Covalently Bound to Coa within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl489 b:37.9 occ:1.00 ND2 B:ASN52 3.2 29.6 1.0 CB B:TYR76 3.3 36.5 1.0 NZ B:LYS329 3.4 47.1 1.0 OE1 B:GLN99 3.4 27.0 1.0 ND2 B:ASN51 3.6 27.8 1.0 CD2 B:TYR76 3.7 43.7 1.0 CE2 B:PHE25 3.7 26.5 1.0 CG B:TYR76 3.7 40.4 1.0 CE B:LYS329 3.8 44.4 1.0 CZ B:PHE25 3.9 26.4 1.0 OG B:SER75 4.1 28.5 1.0 CG B:ASN52 4.1 32.0 1.0 OD1 B:ASN52 4.3 29.9 1.0 CD B:GLN99 4.5 18.5 1.0 CG B:ASN51 4.5 32.5 1.0 OD1 B:ASN51 4.6 31.8 1.0 CD2 B:PHE25 4.6 24.0 1.0 CA B:TYR76 4.7 35.2 1.0 CE2 B:TYR76 4.7 47.3 1.0 CD1 B:TYR76 4.8 46.8 1.0 O B:ALA327 4.9 32.4 1.0 CE1 B:PHE25 4.9 28.2 1.0 CA B:GLY385 4.9 28.8 1.0 N B:TYR76 4.9 34.4 1.0

Chlorine binding site 2 out of 3 in the Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart Covalently Bound to Coa


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart Covalently Bound to Coa within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl489 b:39.4 occ:1.00 ND2 C:ASN52 3.3 16.3 1.0 NZ C:LYS329 3.4 35.4 1.0 CB C:TYR76 3.4 35.5 1.0 OE1 C:GLN99 3.4 24.4 1.0 CE2 C:PHE25 3.6 26.1 1.0 ND2 C:ASN51 3.7 17.0 1.0 CD2 C:TYR76 3.7 42.1 1.0 CE C:LYS329 3.7 33.6 1.0 CG C:TYR76 3.8 37.5 1.0 CZ C:PHE25 3.8 26.4 1.0 OG C:SER75 4.2 28.0 1.0 CG C:ASN52 4.2 25.6 1.0 OD1 C:ASN52 4.3 26.8 1.0 CD C:GLN99 4.5 16.0 1.0 CG C:ASN51 4.6 24.1 1.0 CD2 C:PHE25 4.6 16.8 1.0 OD1 C:ASN51 4.6 23.9 1.0 O C:ALA327 4.7 32.4 1.0 CE2 C:TYR76 4.7 46.0 1.0 CA C:TYR76 4.8 34.4 1.0 CE1 C:PHE25 4.8 24.3 1.0 CD1 C:TYR76 4.8 40.8 1.0

Chlorine binding site 3 out of 3 in the Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart Covalently Bound to Coa


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart Covalently Bound to Coa within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl489 b:36.2 occ:1.00 O D:HOH531 2.9 36.7 1.0 ND2 D:ASN52 3.3 30.5 1.0 CB D:TYR76 3.4 34.0 1.0 NZ D:LYS329 3.4 43.2 1.0 OE1 D:GLN99 3.6 24.7 1.0 CD2 D:TYR76 3.6 45.3 1.0 CE2 D:PHE25 3.7 21.9 1.0 ND2 D:ASN51 3.7 20.1 1.0 CG D:TYR76 3.7 39.7 1.0 CZ D:PHE25 3.8 21.6 1.0 CE D:LYS329 3.8 42.5 1.0 CG D:ASN52 4.2 31.0 1.0 OG D:SER75 4.3 26.6 1.0 OD1 D:ASN52 4.3 29.6 1.0 CD D:GLN99 4.6 23.0 1.0 CD2 D:PHE25 4.6 20.3 1.0 CE2 D:TYR76 4.6 47.3 1.0 CG D:ASN51 4.6 22.7 1.0 CA D:TYR76 4.7 33.4 1.0 OD1 D:ASN51 4.7 18.5 1.0 O D:ALA327 4.7 34.9 1.0 CD1 D:TYR76 4.8 42.5 1.0 CE1 D:PHE25 4.8 25.2 1.0 CA D:GLY385 4.9 26.7 1.0

M.E.Fraser, K.Hayakawa, W.D.Brown. Catalytic Role of the Conformational Change in Succinyl-Coa:3-Oxoacid Coa Transferase on Binding Coa. Biochemistry V. 49 10319 2010.
ISSN: ISSN 0006-2960
PubMed: 20977214
DOI: 10.1021/BI100659S