1CQ6: Aspartate Aminotransferase Complex With C4-Pyridoxal-5p-Phosphate

Domain movement is sometimes essential for substrate recognition by an enzyme. X-ray crystallography of aminotransferase with a series of aliphatic substrates showed that the domain movement of aspartate aminotransferase was changed dramatically from an open to a closed form by the addition of only one CH(2) to the side chain of the C4 substrate CH(3)(CH(2))C((alpha))H(NH(3)(+))COO(-). These crystallographic results and reaction kinetics (Kawaguchi, S., Nobe, Y., Yasuoka, J., Wakamiya, T., Kusumoto, S., and Kuramitsu, S. (1997) J. Biochem. (Tokyo) 122, 55-63; Kawaguchi, S. and Kuramitsu, S. (1998) J. Biol. Chem. 273, 18353-18364) enabled us to estimate the free energy required for the domain movement.
PDB ID: 1CQ6Download
MMDB ID: 15016
PDB Deposition Date: 1999/8/6
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 2.7  Å
Source Organism:
Similar Structures:
Biological Unit for 1CQ6: dimeric; determined by author and by software (PISA,PQS)
Molecular Components in 1CQ6
Label Count Molecule
Proteins (2 molecules)
Aspartate Aminotransferase(Gene symbol: aspC)
Molecule annotation
Chemicals (2 molecules)
* Click molecule labels to explore molecular sequence information.

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