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Zinc in PDB 3tw6: Structure of Rhizobium Etli Pyruvate Carboxylase T882A with the Allosteric Activator, Acetyl Coenzyme-A

Enzymatic activity of Structure of Rhizobium Etli Pyruvate Carboxylase T882A with the Allosteric Activator, Acetyl Coenzyme-A

All present enzymatic activity of Structure of Rhizobium Etli Pyruvate Carboxylase T882A with the Allosteric Activator, Acetyl Coenzyme-A:
6.4.1.1;

Protein crystallography data

The structure of Structure of Rhizobium Etli Pyruvate Carboxylase T882A with the Allosteric Activator, Acetyl Coenzyme-A, PDB code: 3tw6 was solved by M.St Maurice, S.Kumar, A.D.Lietzan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.43 / 2.40
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 370.445, 91.550, 261.354, 90.00, 134.71, 90.00
R / Rfree (%) 18.9 / 23.5

Other elements in 3tw6:

The structure of Structure of Rhizobium Etli Pyruvate Carboxylase T882A with the Allosteric Activator, Acetyl Coenzyme-A also contains other interesting chemical elements:

Magnesium (Mg) 7 atoms
Chlorine (Cl) 8 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Rhizobium Etli Pyruvate Carboxylase T882A with the Allosteric Activator, Acetyl Coenzyme-A (pdb code 3tw6). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Structure of Rhizobium Etli Pyruvate Carboxylase T882A with the Allosteric Activator, Acetyl Coenzyme-A, PDB code: 3tw6:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 3tw6

Go back to Zinc Binding Sites List in 3tw6
Zinc binding site 1 out of 4 in the Structure of Rhizobium Etli Pyruvate Carboxylase T882A with the Allosteric Activator, Acetyl Coenzyme-A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Rhizobium Etli Pyruvate Carboxylase T882A with the Allosteric Activator, Acetyl Coenzyme-A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn2001

b:38.6
occ:1.00
 OD2 A:ASP549 2.1 24.6 1.0
NE2 A:HIS747 2.2 16.3 1.0
NE2 A:HIS749 2.3 25.1 1.0
OQ2 A:KCX718 2.3 21.1 1.0
O A:HOH1251 2.4 19.6 1.0
OQ1 A:KCX718 2.4 24.1 1.0
CX A:KCX718 2.8 21.6 1.0
CG A:ASP549 3.0 22.8 1.0
CE1 A:HIS747 3.0 16.0 1.0
CE1 A:HIS749 3.2 20.3 1.0
OD1 A:ASP549 3.3 23.8 1.0
CD2 A:HIS747 3.3 16.0 1.0
CD2 A:HIS749 3.3 23.3 1.0
NE2 A:GLN783 3.8 18.0 1.0
O A:HOH1208 3.9 25.8 1.0
NH1 A:ARG548 4.0 17.7 1.0
NZ A:KCX718 4.1 22.5 1.0
O A:HOH1250 4.1 27.2 1.0
ND1 A:HIS747 4.2 15.8 1.0
ND1 A:HIS749 4.3 22.9 1.0
CB A:ASP549 4.4 20.6 1.0
O A:HOH1178 4.4 19.3 1.0
CG A:HIS747 4.4 17.2 1.0
CG A:HIS749 4.4 23.2 1.0
CD A:GLN783 4.9 18.8 1.0
CA A:MET720 4.9 21.1 1.0
CZ A:ARG548 4.9 17.8 1.0

Zinc binding site 2 out of 4 in 3tw6

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Zinc binding site 2 out of 4 in the Structure of Rhizobium Etli Pyruvate Carboxylase T882A with the Allosteric Activator, Acetyl Coenzyme-A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Rhizobium Etli Pyruvate Carboxylase T882A with the Allosteric Activator, Acetyl Coenzyme-A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn2001

b:40.5
occ:1.00
 NE2 B:HIS749 2.1 22.0 1.0
OQ1 B:KCX718 2.1 25.4 1.0
OD2 B:ASP549 2.2 25.2 1.0
NE2 B:HIS747 2.2 15.7 1.0
OQ2 B:KCX718 2.3 26.8 1.0
O B:HOH1376 2.4 29.6 1.0
CX B:KCX718 2.6 25.7 1.0
CE1 B:HIS749 2.9 20.1 1.0
CG B:ASP549 3.1 23.6 1.0
CE1 B:HIS747 3.1 16.7 1.0
CD2 B:HIS749 3.2 21.4 1.0
OD1 B:ASP549 3.3 25.2 1.0
CD2 B:HIS747 3.3 16.3 1.0
NE2 B:GLN783 3.9 17.3 1.0
NZ B:KCX718 3.9 24.9 1.0
ND1 B:HIS749 4.1 22.1 1.0
NH1 B:ARG548 4.1 19.8 1.0
O B:HOH1377 4.3 30.1 1.0
CG B:HIS749 4.3 21.6 1.0
ND1 B:HIS747 4.3 16.9 1.0
O B:HOH1162 4.4 25.7 1.0
CB B:ASP549 4.4 21.0 1.0
CG B:HIS747 4.4 17.1 1.0
CA B:MET720 4.8 18.9 1.0
CD B:GLN783 4.9 20.0 1.0
CE B:KCX718 5.0 23.9 1.0

Zinc binding site 3 out of 4 in 3tw6

Go back to Zinc Binding Sites List in 3tw6
Zinc binding site 3 out of 4 in the Structure of Rhizobium Etli Pyruvate Carboxylase T882A with the Allosteric Activator, Acetyl Coenzyme-A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Structure of Rhizobium Etli Pyruvate Carboxylase T882A with the Allosteric Activator, Acetyl Coenzyme-A within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn2001

b:41.7
occ:1.00
 OD2 C:ASP549 2.2 20.9 1.0
OQ1 C:KCX718 2.2 24.8 1.0
NE2 C:HIS747 2.2 18.5 1.0
NE2 C:HIS749 2.3 25.8 1.0
OQ2 C:KCX718 2.3 21.3 1.0
O C:HOH1160 2.4 23.4 1.0
CX C:KCX718 2.6 22.7 1.0
CG C:ASP549 3.0 23.3 1.0
CE1 C:HIS747 3.1 18.4 1.0
CE1 C:HIS749 3.1 22.0 1.0
CD2 C:HIS747 3.2 18.2 1.0
OD1 C:ASP549 3.4 24.0 1.0
CD2 C:HIS749 3.4 22.0 1.0
O C:HOH1290 3.8 32.2 1.0
NE2 C:GLN783 3.9 18.5 1.0
NZ C:KCX718 4.0 23.4 1.0
NH1 C:ARG548 4.2 22.1 1.0
ND1 C:HIS747 4.2 18.1 1.0
ND1 C:HIS749 4.3 21.9 1.0
CG C:HIS747 4.3 18.4 1.0
CB C:ASP549 4.4 20.4 1.0
O C:HOH1221 4.4 24.8 1.0
CG C:HIS749 4.5 22.6 1.0
CA C:MET720 4.9 22.1 1.0
CE C:KCX718 4.9 23.3 1.0

Zinc binding site 4 out of 4 in 3tw6

Go back to Zinc Binding Sites List in 3tw6
Zinc binding site 4 out of 4 in the Structure of Rhizobium Etli Pyruvate Carboxylase T882A with the Allosteric Activator, Acetyl Coenzyme-A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Structure of Rhizobium Etli Pyruvate Carboxylase T882A with the Allosteric Activator, Acetyl Coenzyme-A within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn2001

b:43.4
occ:1.00
 NE2 D:HIS747 2.1 20.0 1.0
OD2 D:ASP549 2.1 25.4 1.0
NE2 D:HIS749 2.2 21.3 1.0
OQ1 D:KCX718 2.2 22.1 1.0
O D:HOH1340 2.4 29.8 1.0
OQ2 D:KCX718 2.4 21.9 1.0
CX D:KCX718 2.7 22.1 1.0
CE1 D:HIS747 3.0 19.9 1.0
CG D:ASP549 3.0 25.5 1.0
CE1 D:HIS749 3.1 20.9 1.0
CD2 D:HIS747 3.1 19.8 1.0
CD2 D:HIS749 3.3 21.2 1.0
OD1 D:ASP549 3.3 26.8 1.0
NE2 D:GLN783 3.8 19.1 1.0
NZ D:KCX718 4.0 20.3 1.0
NH1 D:ARG548 4.1 17.9 1.0
ND1 D:HIS747 4.2 21.1 1.0
CG D:HIS747 4.2 20.7 1.0
ND1 D:HIS749 4.3 23.9 1.0
CG D:HIS749 4.4 22.2 1.0
CB D:ASP549 4.4 21.8 1.0
O D:HOH1282 4.4 25.5 1.0
CA D:MET720 4.8 17.9 1.0
CE D:KCX718 4.9 20.0 1.0
CD D:GLN783 4.9 20.3 1.0

Reference:

A.D.Lietzan, A.L.Menefee, T.N.Zeczycki, S.Kumar, P.V.Attwood, J.C.Wallace, W.W.Cleland, M.St Maurice. Interaction Between the Biotin Carboxyl Carrier Domain and the Biotin Carboxylase Domain in Pyruvate Carboxylase From Rhizobium Etli. Biochemistry V. 50 9708 2011.
ISSN: ISSN 0006-2960
PubMed: 21958016
DOI: 10.1021/BI201277J
Page generated: Sat Oct 26 16:48:11 2024

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