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Literature summary extracted from

  • Vyas, N.K.; Vyas, M.N.; Quiocho, F.A.
    Crystal structure of M tuberculosis ABC phosphate transport receptor: specificity and charge compensation dominated by ion-dipole interactions (2003), Structure, 11, 765-774.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
7.3.2.1 MIR method Mycobacterium tuberculosis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.3.2.1 cell wall on the surface of the outer Mycobacterium tuberculosis 5618
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
7.3.2.1 38000
-
 SDS-PAGE Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.3.2.1 ATP + H2O + phosphate/out Mycobacterium tuberculosis import of phosphate ADP + phosphate + phosphate/in
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
7.3.2.1 Mycobacterium tuberculosis
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
7.3.2.1 no modification
-
 Mycobacterium tuberculosis

Purification (Commentary)

EC Number Purification (Comment) Organism
7.3.2.1
-
 Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.3.2.1 ATP + H2O + phosphate/out import of phosphate Mycobacterium tuberculosis ADP + phosphate + phosphate/in
-
 ?

Synonyms

EC Number Synonyms Comment Organism
7.3.2.1 ABC phosphate transport receptor
-
 Mycobacterium tuberculosis
7.3.2.1 phosphate-bound PstS-1
-
 Mycobacterium tuberculosis
7.3.2.1 phosphate-specific transport substrate binding protein-1
-
 Mycobacterium tuberculosis
7.3.2.1 Pst
-
 Mycobacterium tuberculosis