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Manganese in PDB 5ckx: Non-Covalent Complex of Dahp Synthase and Chorismate Mutase From Mycobacterium Tuberculosis with Bound Transition State Analog and Feedback Effectors Tyrosine and Phenylalanine
Enzymatic activity of Non-Covalent Complex of Dahp Synthase and Chorismate Mutase From Mycobacterium Tuberculosis with Bound Transition State Analog and Feedback Effectors Tyrosine and Phenylalanine
All present enzymatic activity of Non-Covalent Complex of Dahp Synthase and Chorismate Mutase From Mycobacterium Tuberculosis with Bound Transition State Analog and Feedback Effectors Tyrosine and Phenylalanine:
2.5.1.54; 5.4.99.5;
2.5.1.54; 5.4.99.5;
Protein crystallography data
The structure of Non-Covalent Complex of Dahp Synthase and Chorismate Mutase From Mycobacterium Tuberculosis with Bound Transition State Analog and Feedback Effectors Tyrosine and Phenylalanine, PDB code: 5ckx
was solved by
S.Munack,
M.Okvist,
U.Krengel,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
| Resolution Low / High (Å) | 58.72 / 2.70 |
| Space group | P 32 2 1 |
| Cell size a, b, c (Å), α, β, γ (°) | 203.397, 203.397, 67.049, 90.00, 90.00, 120.00 |
| R / Rfree (%) | 20 / 24.9 |
Other elements in 5ckx:
The structure of Non-Covalent Complex of Dahp Synthase and Chorismate Mutase From Mycobacterium Tuberculosis with Bound Transition State Analog and Feedback Effectors Tyrosine and Phenylalanine also contains other interesting chemical elements:
| Chlorine | (Cl) | 3 atoms |
Manganese Binding Sites:
The binding sites of Manganese atom in the Non-Covalent Complex of Dahp Synthase and Chorismate Mutase From Mycobacterium Tuberculosis with Bound Transition State Analog and Feedback Effectors Tyrosine and Phenylalanine
(pdb code 5ckx). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Non-Covalent Complex of Dahp Synthase and Chorismate Mutase From Mycobacterium Tuberculosis with Bound Transition State Analog and Feedback Effectors Tyrosine and Phenylalanine, PDB code: 5ckx:
Jump to Manganese binding site number: 1; 2;
In total 2 binding sites of Manganese where determined in the Non-Covalent Complex of Dahp Synthase and Chorismate Mutase From Mycobacterium Tuberculosis with Bound Transition State Analog and Feedback Effectors Tyrosine and Phenylalanine, PDB code: 5ckx:
Jump to Manganese binding site number: 1; 2;
Manganese binding site 1 out of 2 in 5ckx
Go back to
Manganese Binding Sites List in 5ckx
Manganese binding site 1 out
of 2 in the Non-Covalent Complex of Dahp Synthase and Chorismate Mutase From Mycobacterium Tuberculosis with Bound Transition State Analog and Feedback Effectors Tyrosine and Phenylalanine
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of Non-Covalent Complex of Dahp Synthase and Chorismate Mutase From Mycobacterium Tuberculosis with Bound Transition State Analog and Feedback Effectors Tyrosine and Phenylalanine within 5.0Å range:
|
Manganese binding site 2 out of 2 in 5ckx
Go back to
Manganese Binding Sites List in 5ckx
Manganese binding site 2 out
of 2 in the Non-Covalent Complex of Dahp Synthase and Chorismate Mutase From Mycobacterium Tuberculosis with Bound Transition State Analog and Feedback Effectors Tyrosine and Phenylalanine
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of Non-Covalent Complex of Dahp Synthase and Chorismate Mutase From Mycobacterium Tuberculosis with Bound Transition State Analog and Feedback Effectors Tyrosine and Phenylalanine within 5.0Å range:
|
Reference:
S.Munack,
K.Roderer,
M.Okvist,
J.Kamarauskaite,
S.Sasso,
A.Van Eerde,
P.Kast,
U.Krengel.
Remote Control By Inter-Enzyme Allostery: A Novel Paradigm For Regulation of the Shikimate Pathway. J.Mol.Biol. V. 428 1237 2016.
ISSN: ESSN 1089-8638
PubMed: 26776476
DOI: 10.1016/J.JMB.2016.01.001
Page generated: Sat Oct 5 23:47:26 2024
ISSN: ESSN 1089-8638
PubMed: 26776476
DOI: 10.1016/J.JMB.2016.01.001
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