ESCHERICHIA COLI DIHYDRODIPICOLINATE REDUCTASE IN COMPLEX WITH NADH AND 2,6 PYRIDINE DICARBOXYLATE
The structure was published by Scapin, G., Reddy, S.G., Zheng, R., and Blanchard, J.S., in 1997 in a paper entitled "Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase in complex with NADH and the inhibitor 2,6-pyridinedicarboxylate." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.6 Å and deposited in 1997.
The experimental data on which the structure is based was also deposited.
This PDB entry contains multiple copies of the structure of DIHYDRODIPICOLINATE REDUCTASE.
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 most likely forms homotetramers.
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: