Atomistry » Chlorine » PDB 4eu6-4f1a » 4eua
Atomistry »
  Chlorine »
    PDB 4eu6-4f1a »
      4eua »

Chlorine in PDB 4eua: Succinyl-Coa:Acetate Coa-Transferase (AARCH6-R228E) in Complex with Coa (Anomalous Dataset)

Enzymatic activity of Succinyl-Coa:Acetate Coa-Transferase (AARCH6-R228E) in Complex with Coa (Anomalous Dataset)

All present enzymatic activity of Succinyl-Coa:Acetate Coa-Transferase (AARCH6-R228E) in Complex with Coa (Anomalous Dataset):
2.8.3.18;

Protein crystallography data

The structure of Succinyl-Coa:Acetate Coa-Transferase (AARCH6-R228E) in Complex with Coa (Anomalous Dataset), PDB code: 4eua was solved by E.A.Mullins, T.J.Kappock, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.64 / 2.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 67.391, 110.484, 119.157, 90.00, 90.00, 90.00
R / Rfree (%) 15.2 / 20.9

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Succinyl-Coa:Acetate Coa-Transferase (AARCH6-R228E) in Complex with Coa (Anomalous Dataset) (pdb code 4eua). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Succinyl-Coa:Acetate Coa-Transferase (AARCH6-R228E) in Complex with Coa (Anomalous Dataset), PDB code: 4eua:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in 4eua

Go back to Chlorine Binding Sites List in 4eua
Chlorine binding site 1 out of 4 in the Succinyl-Coa:Acetate Coa-Transferase (AARCH6-R228E) in Complex with Coa (Anomalous Dataset)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Succinyl-Coa:Acetate Coa-Transferase (AARCH6-R228E) in Complex with Coa (Anomalous Dataset) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl516

b:43.2
occ:1.00
 NH2 B:ARG354 3.2 20.8 1.0
NH2 A:ARG354 3.3 17.5 1.0
O A:HOH967 3.3 31.6 1.0
O B:HOH750 3.5 17.9 1.0
N A:VAL196 3.6 23.3 1.0
O A:VAL196 4.2 26.9 1.0
CZ B:ARG354 4.2 15.8 1.0
CA A:ILE195 4.2 18.7 1.0
NE B:ARG354 4.2 13.6 1.0
CG2 A:VAL196 4.2 21.0 1.0
CG2 A:ILE195 4.3 16.8 1.0
C A:ILE195 4.4 21.7 1.0
CZ A:ARG354 4.4 12.8 1.0
CB A:VAL196 4.5 33.8 1.0
CA A:VAL196 4.5 24.0 1.0
C A:VAL196 4.7 23.1 1.0
NH1 A:ARG354 4.7 15.6 1.0
CB A:ILE195 4.8 18.5 1.0
O A:ASP194 4.8 18.1 1.0
CL B:CL516 4.9 26.4 1.0

Chlorine binding site 2 out of 4 in 4eua

Go back to Chlorine Binding Sites List in 4eua
Chlorine binding site 2 out of 4 in the Succinyl-Coa:Acetate Coa-Transferase (AARCH6-R228E) in Complex with Coa (Anomalous Dataset)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Succinyl-Coa:Acetate Coa-Transferase (AARCH6-R228E) in Complex with Coa (Anomalous Dataset) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl515

b:22.7
occ:1.00
 O A:HOH576 2.9 13.1 1.0
ND2 A:ASN125 3.1 12.2 1.0
N B:GLY443 3.3 9.1 1.0
NH1 A:ARG120 3.4 10.4 1.0
ND2 A:ASN112 3.6 13.2 1.0
OD1 A:ASN112 3.6 10.8 1.0
CD A:ARG120 3.6 11.4 1.0
CB A:ASN125 3.8 9.8 1.0
CA B:GLY443 3.8 11.8 1.0
CG A:ASN125 3.9 13.8 1.0
CG A:ASN112 4.0 15.8 1.0
C B:ARG442 4.3 10.4 1.0
CA B:ARG442 4.4 12.9 1.0
CZ A:ARG120 4.4 11.6 1.0
NE A:ARG120 4.5 12.4 1.0
CE2 A:PHE110 4.5 6.9 1.0
CD2 A:PHE110 4.5 7.5 1.0
CB A:ARG120 4.7 11.8 1.0
CG A:ARG120 4.7 10.0 1.0
O B:HOH529 4.8 7.4 1.0
C B:GLY443 4.9 13.6 1.0
CB B:ARG442 5.0 11.9 1.0

Chlorine binding site 3 out of 4 in 4eua

Go back to Chlorine Binding Sites List in 4eua
Chlorine binding site 3 out of 4 in the Succinyl-Coa:Acetate Coa-Transferase (AARCH6-R228E) in Complex with Coa (Anomalous Dataset)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Succinyl-Coa:Acetate Coa-Transferase (AARCH6-R228E) in Complex with Coa (Anomalous Dataset) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl516

b:26.4
occ:1.00
 O A:HOH967 2.8 31.6 1.0
O A:HOH681 2.9 31.6 1.0
N B:VAL196 3.1 19.6 1.0
NH2 B:ARG354 3.2 20.8 1.0
CG2 B:VAL196 3.7 19.0 1.0
O B:VAL196 3.7 28.8 1.0
CB B:VAL196 3.8 35.1 1.0
NH2 A:ARG354 3.9 17.5 1.0
CA B:VAL196 3.9 21.3 1.0
CA B:ILE195 4.0 16.6 1.0
C B:ILE195 4.0 19.2 1.0
CZ B:ARG354 4.2 15.8 1.0
CG2 B:ILE195 4.2 15.7 1.0
C B:VAL196 4.2 20.1 1.0
NH1 B:ARG354 4.3 10.9 1.0
O A:HOH646 4.3 14.6 1.0
O B:ASP194 4.5 16.8 1.0
CB B:ILE195 4.6 18.7 1.0
CG1 B:ILE351 4.7 11.1 1.0
NE A:ARG354 4.8 11.8 1.0
CZ A:ARG354 4.8 12.8 1.0
CL A:CL516 4.9 43.2 1.0

Chlorine binding site 4 out of 4 in 4eua

Go back to Chlorine Binding Sites List in 4eua
Chlorine binding site 4 out of 4 in the Succinyl-Coa:Acetate Coa-Transferase (AARCH6-R228E) in Complex with Coa (Anomalous Dataset)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Succinyl-Coa:Acetate Coa-Transferase (AARCH6-R228E) in Complex with Coa (Anomalous Dataset) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl515

b:17.7
occ:1.00
 O A:HOH833 3.1 13.9 1.0
ND2 B:ASN125 3.2 10.8 1.0
N A:GLY443 3.2 8.5 1.0
NH1 B:ARG120 3.4 8.0 1.0
OD1 B:ASN112 3.6 18.0 1.0
ND2 B:ASN112 3.7 13.5 1.0
CD B:ARG120 3.7 9.3 1.0
CB B:ASN125 3.9 12.4 1.0
CA A:GLY443 3.9 10.2 1.0
CG B:ASN125 4.0 11.5 1.0
CG B:ASN112 4.1 15.9 1.0
C A:ARG442 4.2 13.5 1.0
CA A:ARG442 4.2 12.1 1.0
CE2 B:PHE110 4.4 9.4 1.0
CZ B:ARG120 4.4 13.9 1.0
CD2 B:PHE110 4.4 8.4 1.0
NE B:ARG120 4.5 15.3 1.0
O A:HOH673 4.7 9.3 1.0
O A:HOH580 4.8 7.5 1.0
CB A:ARG442 4.8 11.0 1.0
CB B:ARG120 4.9 9.8 1.0
CG B:ARG120 4.9 10.0 1.0
C A:GLY443 5.0 11.6 1.0

Reference:

E.A.Mullins, T.J.Kappock. Crystal Structures of Acetobacter Aceti Succinyl-Coenzyme A (Coa):Acetate Coa-Transferase Reveal Specificity Determinants and Illustrate the Mechanism Used By Class I Coa-Transferases. Biochemistry V. 51 8422 2012.
ISSN: ISSN 0006-2960
PubMed: 23030530
DOI: 10.1021/BI300957F
Page generated: Sun Jul 21 13:21:22 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy