1dio Summary

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DIOL DEHYDRATASE-CYANOCOBALAMIN COMPLEX FROM KLEBSIELLA OXYTOCA

The structure was published by Shibata, N., Masuda, J., Tobimatsu, T., et al., Suto, K., Morimoto, Y., and Yasuoka, N., in 1999 in a paper entitled "A new mode of B12 binding and the direct participation of a potassium ion in enzyme catalysis: X-ray structure of diol dehydratase." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 1999.

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

This PDB entry contains a complex of 3 biomacromolecules, namely PROTEIN (DIOL DEHYDRATASE).

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 heterohexamers.

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 PROTEIN (DIOL DEHYDRATASE) Q59470 (1-554) (Q59470_KLEOX)search Klebsiella oxytocasearch 100% 554 99%
L PROTEIN (DIOL DEHYDRATASE) Q59470 (1-554) (Q59470_KLEOX)search Klebsiella oxytocasearch 100% 554 99%
B PROTEIN (DIOL DEHYDRATASE) Q59471 (1-224) (Q59471_KLEOX)search Klebsiella oxytocasearch 100% 224 79%
E PROTEIN (DIOL DEHYDRATASE) Q59471 (1-224) (Q59471_KLEOX)search Klebsiella oxytocasearch 100% 224 79%
G PROTEIN (DIOL DEHYDRATASE) Q59472 (1-173) (Q59472_KLEOX)search Klebsiella oxytocasearch 100% 173 79%
M PROTEIN (DIOL DEHYDRATASE) Q59472 (1-173) (Q59472_KLEOX)search Klebsiella oxytocasearch 100% 173 79%


This entry contains 3 unique UniProt proteins:

UniProt accession Name Organism PDB
Q59470 (1 - 554) PROTEIN (DIOL DEHYDRATASE) Klebsiella oxytoca
Q59471 (1 - 224) PROTEIN (DIOL DEHYDRATASE) Klebsiella oxytoca
Q59472 (1 - 173) PROTEIN (DIOL DEHYDRATASE) Klebsiella oxytoca

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, L (Q59470) Diol dehydratase, alpha subunitsearch TIM Barrelsearch PF02286: Dehydratase large subunitsearch
B, E (Q59471) Diol dehydratase, beta subunitsearch Diol Dehydratase; Chain Bsearch PF02288: Dehydratase medium subunitsearch
G, M (Q59472) Diol dehydratase, gamma subunitsearch PF02287: Dehydratase small subunitsearch

Chain ID Biological process (GO) Molecular function (GO)
A, L (Q59470) metabolic processsearch cobalamin bindingsearch catalytic activitysearch hydro-lyase activitysearch propanediol dehydratase activitysearch metal ion bindingsearch lyase activitysearch
B, E (Q59471) metabolic processsearch propanediol dehydratase activitysearch lyase activitysearch
G, M (Q59472) metabolic processsearch propanediol dehydratase activitysearch lyase activitysearch

Chain InterPro annotation
A, L Diol/glycerol dehydratase, large subunitsearch Cobalamin (vitamin B12)-dependent enzyme, catalyticsearch
B, E Diol/glycerol dehydratase/dehydratase reactivating factorsearch B12-dependent dehydratases, beta subunitsearch Propanediol/glycerol dehydratase, medium subunitsearch
G, M Propanediol/glycerol dehydratase, small subunitsearch