Crystal structure of the Apo form of D-alanine: D-alanine ligase (Ddl) from Thermus caldophilus: a basis for the substrate-induced conformational changes
The structure was published by Lee, J.H., Na, Y., Song, H.E., et al., Kang, G.B., Lee, D.S., and Eom, S.H., in 2006 in a paper entitled "Crystal structure of the apo form of D-alanine: D-alanine ligase (Ddl) from Thermus caldophilus: A basis for the substrate-induced conformational changes" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 2005.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of D-alanine:D-alanine ligase. This molecule has the UniProt identifier Q3T920 (Q3T920_THECA). The sample contained 322 residues which is 100% of the natural sequence. Out of 322 residues 322 were observed and are deposited in the PDB.
The molecule most likely forms homodimers.
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):
This entry contains 1 unique UniProt protein: