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Chlorine in PDB 3glm: Glutaconyl-Coa Decarboxylase A Subunit From Clostridium Symbiosum Co- Crystallized with Crotonyl-Coa

Enzymatic activity of Glutaconyl-Coa Decarboxylase A Subunit From Clostridium Symbiosum Co- Crystallized with Crotonyl-Coa

All present enzymatic activity of Glutaconyl-Coa Decarboxylase A Subunit From Clostridium Symbiosum Co- Crystallized with Crotonyl-Coa:
4.1.1.70;

Protein crystallography data

The structure of Glutaconyl-Coa Decarboxylase A Subunit From Clostridium Symbiosum Co- Crystallized with Crotonyl-Coa, PDB code: 3glm was solved by D.Kress, D.Brugel, W.Buckel, L.-O.Essen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.76 / 2.50
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 101.500, 167.450, 138.110, 90.00, 89.98, 90.00
R / Rfree (%) 19.3 / 23

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Glutaconyl-Coa Decarboxylase A Subunit From Clostridium Symbiosum Co- Crystallized with Crotonyl-Coa (pdb code 3glm). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Glutaconyl-Coa Decarboxylase A Subunit From Clostridium Symbiosum Co- Crystallized with Crotonyl-Coa, PDB code: 3glm:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in 3glm

Go back to Chlorine Binding Sites List in 3glm
Chlorine binding site 1 out of 4 in the Glutaconyl-Coa Decarboxylase A Subunit From Clostridium Symbiosum Co- Crystallized with Crotonyl-Coa


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Glutaconyl-Coa Decarboxylase A Subunit From Clostridium Symbiosum Co- Crystallized with Crotonyl-Coa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl589

b:46.3
occ:1.00
 O A:HOH699 2.9 25.2 1.0
N A:ILE420 3.1 34.6 1.0
N A:ALA460 3.4 30.1 1.0
CB A:ALA460 3.5 30.2 1.0
N A:ALA461 3.5 29.0 1.0
CB A:ALA459 3.6 29.8 1.0
CB A:ILE420 3.7 34.7 1.0
CA A:ALA460 3.7 29.9 1.0
CA A:GLY419 3.8 33.7 1.0
CG1 C:VAL217 3.9 37.1 1.0
C A:ALA460 3.9 29.5 1.0
CG1 A:ILE420 4.0 35.2 1.0
CA A:ILE420 4.0 34.9 1.0
C A:GLY419 4.0 34.2 1.0
CD1 A:ILE420 4.0 35.5 1.0
C A:ALA459 4.3 30.2 1.0
O C:HOH725 4.3 23.7 1.0
O A:ILE420 4.4 35.1 1.0
CA A:ALA461 4.4 28.8 1.0
CB A:ALA461 4.4 28.8 1.0
CA A:ALA459 4.5 30.1 1.0
C A:ILE420 4.7 35.2 1.0
O C:VAL217 4.9 39.5 1.0
O A:ALA460 4.9 29.4 1.0
CG2 A:ILE420 5.0 34.1 1.0
CE1 C:TYR199 5.0 35.6 1.0

Chlorine binding site 2 out of 4 in 3glm

Go back to Chlorine Binding Sites List in 3glm
Chlorine binding site 2 out of 4 in the Glutaconyl-Coa Decarboxylase A Subunit From Clostridium Symbiosum Co- Crystallized with Crotonyl-Coa


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Glutaconyl-Coa Decarboxylase A Subunit From Clostridium Symbiosum Co- Crystallized with Crotonyl-Coa within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl589

b:38.4
occ:1.00
 O D:HOH702 2.9 31.8 1.0
N B:ILE420 3.2 34.5 1.0
N B:ALA460 3.3 30.2 1.0
CB B:ALA460 3.4 30.3 1.0
N B:ALA461 3.4 28.9 1.0
CB B:ILE420 3.7 34.6 1.0
CB B:ALA459 3.7 29.9 1.0
CA B:ALA460 3.7 29.9 1.0
C B:ALA460 3.9 29.5 1.0
CG1 B:ILE420 3.9 35.2 1.0
CG1 D:VAL217 3.9 37.1 1.0
CA B:GLY419 3.9 33.7 1.0
CD1 B:ILE420 3.9 35.4 1.0
CA B:ILE420 4.0 34.9 1.0
C B:GLY419 4.1 34.1 1.0
C B:ALA459 4.3 30.2 1.0
CA B:ALA461 4.3 28.7 1.0
CB B:ALA461 4.4 28.9 1.0
O B:ILE420 4.5 35.1 1.0
CA B:ALA459 4.6 30.1 1.0
C B:ILE420 4.7 35.2 1.0
O B:ALA460 4.9 29.4 1.0
CE1 D:TYR199 4.9 35.6 1.0
O D:VAL217 4.9 39.4 1.0
CG2 B:ILE420 5.0 34.2 1.0

Chlorine binding site 3 out of 4 in 3glm

Go back to Chlorine Binding Sites List in 3glm
Chlorine binding site 3 out of 4 in the Glutaconyl-Coa Decarboxylase A Subunit From Clostridium Symbiosum Co- Crystallized with Crotonyl-Coa


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Glutaconyl-Coa Decarboxylase A Subunit From Clostridium Symbiosum Co- Crystallized with Crotonyl-Coa within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl589

b:45.1
occ:1.00
 O C:HOH613 3.0 30.6 1.0
N C:ILE420 3.2 34.5 1.0
N C:ALA460 3.4 30.1 1.0
N C:ALA461 3.4 29.0 1.0
CB C:ALA460 3.4 30.1 1.0
CB C:ILE420 3.6 34.6 1.0
CA C:ALA460 3.7 29.9 1.0
CB C:ALA459 3.7 29.8 1.0
CG1 A:VAL217 3.9 37.0 1.0
CG1 C:ILE420 3.9 35.2 1.0
C C:ALA460 3.9 29.6 1.0
CD1 C:ILE420 3.9 35.5 1.0
CA C:GLY419 3.9 33.6 1.0
CA C:ILE420 4.0 34.8 1.0
C C:GLY419 4.0 34.1 1.0
C C:ALA459 4.3 30.2 1.0
CA C:ALA461 4.3 28.7 1.0
O C:ILE420 4.4 35.0 1.0
CB C:ALA461 4.4 28.7 1.0
O A:HOH716 4.5 24.2 1.0
CA C:ALA459 4.6 30.1 1.0
C C:ILE420 4.7 35.2 1.0
CE1 A:TYR199 4.9 35.6 1.0
O C:ALA460 4.9 29.4 1.0
CG2 C:ILE420 4.9 34.1 1.0
O A:VAL217 4.9 39.4 1.0

Chlorine binding site 4 out of 4 in 3glm

Go back to Chlorine Binding Sites List in 3glm
Chlorine binding site 4 out of 4 in the Glutaconyl-Coa Decarboxylase A Subunit From Clostridium Symbiosum Co- Crystallized with Crotonyl-Coa


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Glutaconyl-Coa Decarboxylase A Subunit From Clostridium Symbiosum Co- Crystallized with Crotonyl-Coa within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl589

b:43.3
occ:1.00
 N D:ILE420 3.2 34.5 1.0
N D:ALA460 3.3 30.2 1.0
N D:ALA461 3.3 28.9 1.0
CB D:ALA460 3.4 30.2 1.0
CB D:ALA459 3.6 29.8 1.0
CB D:ILE420 3.7 34.7 1.0
CA D:ALA460 3.7 29.8 1.0
C D:ALA460 3.8 29.5 1.0
CA D:GLY419 3.8 33.6 1.0
CG1 D:ILE420 3.9 35.2 1.0
CG1 B:VAL217 4.0 37.0 1.0
CA D:ILE420 4.0 34.8 1.0
C D:GLY419 4.0 34.1 1.0
CD1 D:ILE420 4.0 35.4 1.0
C D:ALA459 4.2 30.2 1.0
CA D:ALA461 4.3 28.7 1.0
CB D:ALA461 4.3 28.8 1.0
O D:ILE420 4.5 35.1 1.0
CA D:ALA459 4.5 30.1 1.0
C D:ILE420 4.7 35.2 1.0
O D:ALA460 4.8 29.3 1.0
CE1 B:TYR199 5.0 35.6 1.0
CG2 D:ILE420 5.0 34.2 1.0
O B:VAL217 5.0 39.4 1.0

Reference:

D.Kress, D.Brugel, I.Schall, D.Linder, W.Buckel, L.-O.Essen. An Asymmetric Model For Na+-Translocating Glutaconyl-Coa Decarboxylases J.Biol.Chem. V. 284 28401 2009.
ISSN: ISSN 0021-9258
PubMed: 19654317
DOI: 10.1074/JBC.M109.037762
Page generated: Fri Jul 11 05:41:56 2025

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