Chlorine in PDB 4u19: Crystal Structure of Human Peroxisomal DELTA3,DELTA2, Enoyl-Coa Isomerase V349A Mutant (Isoa-ECI2)

All present enzymatic activity of Crystal Structure of Human Peroxisomal DELTA3,DELTA2, Enoyl-Coa Isomerase V349A Mutant (Isoa-ECI2):
5.3.3.8;

The structure of Crystal Structure of Human Peroxisomal DELTA3,DELTA2, Enoyl-Coa Isomerase V349A Mutant (Isoa-ECI2), PDB code: 4u19 was solved by G.U.Onwukwe, M.K.Koski, R.K.Wierenga, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.60 / 1.88
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	47.609, 123.690, 128.933, 90.00, 90.00, 90.00
R / Rfree (%)	18.4 / 23.4

The binding sites of Chlorine atom in the Crystal Structure of Human Peroxisomal DELTA3,DELTA2, Enoyl-Coa Isomerase V349A Mutant (Isoa-ECI2) (pdb code 4u19). 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 Human Peroxisomal DELTA3,DELTA2, Enoyl-Coa Isomerase V349A Mutant (Isoa-ECI2), PDB code: 4u19:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of Human Peroxisomal DELTA3,DELTA2, Enoyl-Coa Isomerase V349A Mutant (Isoa-ECI2)


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 Peroxisomal DELTA3,DELTA2, Enoyl-Coa Isomerase V349A Mutant (Isoa-ECI2) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl401 b:71.4 occ:1.00 O A:ASN185 4.2 27.0 1.0 CE2 A:TYR134 4.3 37.5 1.0 CB A:ASN185 4.3 32.4 1.0 OD1 A:ASN165 4.3 41.2 1.0 CZ A:TYR134 4.4 35.5 1.0 CG A:ASN185 4.4 39.0 1.0 OH A:TYR134 4.5 38.1 1.0 OD1 A:ASN185 4.5 39.0 1.0 CH2 A:TRP340 4.7 38.0 1.0 CA A:ASN185 4.7 28.9 1.0 C A:ASN185 4.8 28.9 1.0 CD2 A:TYR134 4.8 34.1 1.0 CZ2 A:TRP340 4.8 42.1 1.0 CD2 A:LEU188 4.8 33.8 1.0 CB A:LEU189 4.9 28.6 1.0 CG A:ASN165 5.0 40.0 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of Human Peroxisomal DELTA3,DELTA2, Enoyl-Coa Isomerase V349A Mutant (Isoa-ECI2)


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 Peroxisomal DELTA3,DELTA2, Enoyl-Coa Isomerase V349A Mutant (Isoa-ECI2) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl401 b:83.3 occ:1.00 O B:ASN185 3.9 40.7 1.0 CB B:ASN185 4.0 46.7 1.0 ND2 B:ASN165 4.1 54.1 1.0 CG B:ASN185 4.2 51.5 1.0 CE2 B:TYR134 4.3 57.6 1.0 CA B:ASN185 4.3 43.8 1.0 CZ B:TYR134 4.3 58.6 1.0 OD1 B:ASN185 4.4 52.6 1.0 OH B:TYR134 4.5 59.3 1.0 C B:ASN185 4.5 39.7 1.0 CH2 B:TRP340 4.6 42.9 1.0 CD2 B:LEU188 4.7 46.9 1.0 CD2 B:TYR134 4.8 47.4 1.0 ND2 B:ASN185 4.8 50.2 1.0 CZ2 B:TRP340 4.9 40.4 1.0 CE1 B:TYR134 4.9 53.2 1.0 CG B:ASN165 4.9 56.9 1.0 OD1 B:ASN165 5.0 58.4 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of Human Peroxisomal DELTA3,DELTA2, Enoyl-Coa Isomerase V349A Mutant (Isoa-ECI2)


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 Peroxisomal DELTA3,DELTA2, Enoyl-Coa Isomerase V349A Mutant (Isoa-ECI2) within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl401 b:89.6 occ:1.00 O C:ASN185 3.3 42.4 1.0 CB C:ASN185 4.0 42.4 1.0 C C:ASN185 4.1 43.8 1.0 CB C:LEU189 4.2 34.2 1.0 CG C:ASN185 4.2 47.6 1.0 CA C:ASN185 4.3 44.7 1.0 CZ C:TYR134 4.3 49.0 1.0 OD1 C:ASN185 4.3 50.4 1.0 CH2 C:TRP340 4.4 48.8 1.0 OH C:TYR134 4.4 50.4 1.0 N C:LEU189 4.4 31.7 1.0 CE1 C:TYR134 4.5 47.8 1.0 CD2 C:LEU188 4.5 38.5 1.0 CA C:LEU189 4.6 34.4 1.0 CE2 C:TYR134 4.6 40.5 1.0 CZ2 C:TRP340 4.7 49.2 1.0 CG C:LEU188 4.8 38.6 1.0 CB C:LEU188 4.9 34.5 1.0 ND2 C:ASN185 4.9 50.5 1.0 CD1 C:TYR134 4.9 46.6 1.0

G.U.Onwukwe, P.Kursula, M.K.Koski, W.Schmitz, R.K.Wierenga. Human Delta 3, DELTA2-Enoyl-Coa Isomerase, Type-2: A Structural Enzymology Study on the Catalytic Role of Its Acbp-Domain and Helix-10. Febs J. 2014.
ISSN: ISSN 1742-464X
DOI: 10.1111/FEBS.13179