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Zinc in PDB 2atc: Crystal and Molecular Structures of Native and Ctp-Liganded Aspartate Carbamoyltransferase From Escherichia Coli

Enzymatic activity of Crystal and Molecular Structures of Native and Ctp-Liganded Aspartate Carbamoyltransferase From Escherichia Coli

All present enzymatic activity of Crystal and Molecular Structures of Native and Ctp-Liganded Aspartate Carbamoyltransferase From Escherichia Coli:
2.1.3.2;

Protein crystallography data

The structure of Crystal and Molecular Structures of Native and Ctp-Liganded Aspartate Carbamoyltransferase From Escherichia Coli, PDB code: 2atc was solved by R.B.Honzatko, J.L.Crawford, H.L.Monaco, J.E.Ladner, B.F.P.Edwards, D.R.Evans, S.G.Warren, D.C.Wiley, R.C.Ladner, W.N.Lipscomb, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 3.00
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 131.700, 131.700, 199.200, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal and Molecular Structures of Native and Ctp-Liganded Aspartate Carbamoyltransferase From Escherichia Coli (pdb code 2atc). 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 Crystal and Molecular Structures of Native and Ctp-Liganded Aspartate Carbamoyltransferase From Escherichia Coli, PDB code: 2atc:

Zinc binding site 1 out of 1 in 2atc

Go back to Zinc Binding Sites List in 2atc
Zinc binding site 1 out of 1 in the Crystal and Molecular Structures of Native and Ctp-Liganded Aspartate Carbamoyltransferase 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 Crystal and Molecular Structures of Native and Ctp-Liganded Aspartate Carbamoyltransferase From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn153

b:20.0
occ:1.00
 SG B:CYS114 1.7 20.0 1.0
SG B:CYS109 1.8 20.0 1.0
SG B:CYS140 1.8 20.0 1.0
SG B:CYS137 2.1 20.0 1.0
CB B:CYS140 3.0 20.0 1.0
CB B:CYS109 3.1 20.0 1.0
CB B:CYS114 3.1 20.0 1.0
CB B:CYS137 3.2 20.0 1.0
N B:CYS140 3.8 20.0 1.0
OG B:SER116 3.9 20.0 1.0
O B:CYS137 3.9 20.0 1.0
CA B:CYS140 4.0 20.0 1.0
CB B:TYR139 4.0 20.0 1.0
CA B:CYS114 4.1 20.0 1.0
O B:CYS140 4.3 20.0 1.0
CA B:CYS109 4.4 20.0 1.0
C B:CYS140 4.5 20.0 1.0
CB B:ASP111 4.5 20.0 1.0
CA B:CYS137 4.6 20.0 1.0
C B:TYR139 4.6 20.0 1.0
OD1 B:ASP111 4.7 20.0 1.0
C B:CYS137 4.8 20.0 1.0
CB B:SER116 4.8 20.0 1.0
CA B:TYR139 4.9 20.0 1.0
N B:CYS114 4.9 20.0 1.0
CE1 B:PHE144 5.0 20.0 1.0
CG B:ASP111 5.0 20.0 1.0

Reference:

R.B.Honzatko, J.L.Crawford, H.L.Monaco, J.E.Ladner, B.F.Ewards, D.R.Evans, S.G.Warren, D.C.Wiley, R.C.Ladner, W.N.Lipscomb. Crystal and Molecular Structures of Native and Ctp-Liganded Aspartate Carbamoyltransferase From Escherichia Coli. J.Mol.Biol. V. 160 219 1982.
ISSN: ISSN 0022-2836
PubMed: 6757446
DOI: 10.1016/0022-2836(82)90175-9
Page generated: Wed Oct 16 21:49:45 2024

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