1mt0 Summary


ATP-binding domain of hemolysin B from Escherichia coli

The structure was published by Schmitt, L., Benabdelhak, H., Blight, M.A., Holland, I.B., and Stubbs, M.T., in 2003 in a paper entitled "Crystal structure of the nucleotide binding domain of the ABC-transporter hemolysin B: identification of a variable region within ABC helical domains" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.6 Å and deposited in 2002.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of Hemolysin secretion ATP-binding protein. This molecule has the UniProt identifier P08716 (HLYBP_ECOLX)search. The sample contained 241 residues which is < 90% of the natural sequence. Out of 241 residues 241 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Hemolysin secretion ATP-binding protein P08716 (467-707) (HLYBP_ECOLX)search Escherichia colisearch < 90% 241 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P08716 (467 - 707) Hemolysin secretion ATP-binding protein Escherichia coli

Chain Structural classification (SCOP) Sequence family (Pfam)
A ABC transporter ATPase domain-likesearch ABC transportersearch

Chain ID Molecular function (GO)
A (P08716) ATP bindingsearch ATPase activitysearch

Chain InterPro annotation
A ABC transporter-likesearch AAA+ ATPase domainsearch ABC transporter, conserved sitesearch P-loop containing nucleoside triphosphate hydrolasesearch