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Atomistry » Zinc » PDB 1pe8-1pud » 1pg5 » |
Zinc in PDB 1pg5: Crystal Structure of the Unligated (T-State) Aspartate Transcarbamoylase From the Extremely Thermophilic Archaeon Sulfolobus AcidocaldariusEnzymatic activity of Crystal Structure of the Unligated (T-State) Aspartate Transcarbamoylase From the Extremely Thermophilic Archaeon Sulfolobus Acidocaldarius
All present enzymatic activity of Crystal Structure of the Unligated (T-State) Aspartate Transcarbamoylase From the Extremely Thermophilic Archaeon Sulfolobus Acidocaldarius:
2.1.3.2; Protein crystallography data
The structure of Crystal Structure of the Unligated (T-State) Aspartate Transcarbamoylase From the Extremely Thermophilic Archaeon Sulfolobus Acidocaldarius, PDB code: 1pg5
was solved by
D.De Vos,
F.Van Petegem,
H.Remaut,
C.Legrain,
N.Glansdorff,
J.J.Vanbeeumen,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of the Unligated (T-State) Aspartate Transcarbamoylase From the Extremely Thermophilic Archaeon Sulfolobus Acidocaldarius
(pdb code 1pg5). 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 Structure of the Unligated (T-State) Aspartate Transcarbamoylase From the Extremely Thermophilic Archaeon Sulfolobus Acidocaldarius, PDB code: 1pg5: Zinc binding site 1 out of 1 in 1pg5Go back to Zinc Binding Sites List in 1pg5
Zinc binding site 1 out
of 1 in the Crystal Structure of the Unligated (T-State) Aspartate Transcarbamoylase From the Extremely Thermophilic Archaeon Sulfolobus Acidocaldarius
Mono view Stereo pair view
Reference:
D.De Vos,
F.Van Petegem,
H.Remaut,
C.Legrain,
N.Glansdorff,
J.J.Van Beeumen.
Crystal Structure of T State Aspartate Carbamoyltransferase of the Hyperthermophilic Archaeon Sulfolobus Acidocaldarius. J.Mol.Biol. V. 339 887 2004.
Page generated: Wed Dec 16 03:00:45 2020
ISSN: ISSN 0022-2836 PubMed: 15165857 DOI: 10.1016/J.JMB.2004.03.079 |
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