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Zinc in PDB 2f9y: The Crystal Structure of the Carboxyltransferase Subunit of Acc From Escherichia Coli

Enzymatic activity of The Crystal Structure of the Carboxyltransferase Subunit of Acc From Escherichia Coli

All present enzymatic activity of The Crystal Structure of the Carboxyltransferase Subunit of Acc From Escherichia Coli:
6.4.1.2;

Protein crystallography data

The structure of The Crystal Structure of the Carboxyltransferase Subunit of Acc From Escherichia Coli, PDB code: 2f9y was solved by P.W.Bilder, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.73 / 3.20
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 156.729, 156.728, 192.824, 90.00, 90.00, 120.00
R / Rfree (%) 25.7 / 26.1

Zinc Binding Sites:

The binding sites of Zinc atom in the The Crystal Structure of the Carboxyltransferase Subunit of Acc From Escherichia Coli (pdb code 2f9y). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the The Crystal Structure of the Carboxyltransferase Subunit of Acc From Escherichia Coli, PDB code: 2f9y:

Zinc binding site 1 out of 1 in 2f9y

Go back to Zinc Binding Sites List in 2f9y
Zinc binding site 1 out of 1 in the The Crystal Structure of the Carboxyltransferase Subunit of Acc From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Crystal Structure of the Carboxyltransferase Subunit of Acc From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn305

b:81.6
occ:1.00
SG B:CYS49 1.7 95.9 1.0
SG B:CYS46 2.2 64.0 1.0
CB B:CYS30 2.3 84.4 1.0
SG B:CYS30 2.6 88.2 1.0
CB B:CYS49 2.9 92.5 1.0
SG B:CYS27 2.9 0.8 1.0
CB B:CYS27 3.6 0.5 1.0
CB B:CYS46 3.7 60.1 1.0
CA B:CYS30 3.8 0.2 1.0
N B:CYS49 3.9 95.3 0.0
CA B:CYS49 4.0 86.4 1.0
CB B:GLN32 4.3 0.7 1.0
O B:SER29 4.3 1.0 1.0
C B:CYS30 4.4 0.3 1.0
N B:CYS30 4.5 0.2 1.0
C B:LYS48 4.6 89.1 1.0
C B:SER29 4.6 0.9 1.0
N B:GLY31 4.6 0.2 1.0
N B:GLN32 4.7 0.5 1.0
CB B:LYS48 4.8 1.0 1.0
CA B:CYS46 4.9 86.9 1.0

Reference:

P.Bilder, S.Lightle, G.Bainbridge, J.Ohren, B.Finzel, F.Sun, S.Holley, L.Al-Kassim, C.Spessard, M.Melnick, M.Newcomer, G.L.Waldrop. The Structure of the Carboxyltransferase Component of Acetyl-Coa Carboxylase Reveals A Zinc-Binding Motif Unique to the Bacterial Enzyme(,). Biochemistry V. 45 1712 2006.
ISSN: ISSN 0006-2960
PubMed: 16460018
DOI: 10.1021/BI0520479
Page generated: Wed Oct 16 23:42:15 2024

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