1ozh Summary

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The crystal structure of Klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate.

The structure was published by Pang, S.S., Duggleby, R.G., Schowen, R.L., and Guddat, L.W., in 2004 in a paper entitled "The Crystal Structures of Klebsiella pneumoniae Acetolactate Synthase with Enzyme-bound Cofactor and with an Unusual Intermediate." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 2003.

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

This PDB entry contains multiple copies of the structure of Acetolactate synthase, catabolic.

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):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Acetolactate synthase, catabolic P27696 (1-559) (ILVB_KLEPN)search Klebsiella pneumoniaesearch 100% 566 96%
B Acetolactate synthase, catabolic P27696 (1-559) (ILVB_KLEPN)search Klebsiella pneumoniaesearch 100% 566 96%
C Acetolactate synthase, catabolic P27696 (1-559) (ILVB_KLEPN)search Klebsiella pneumoniaesearch 100% 566 96%
D Acetolactate synthase, catabolic P27696 (1-559) (ILVB_KLEPN)search Klebsiella pneumoniaesearch 100% 566 96%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P27696 (1 - 559) Acetolactate synthase, catabolic Klebsiella pneumoniae

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B, C, D (P27696) Pyruvate oxidase and decarboxylase, middle domainsearch, Pyruvate oxidase and decarboxylase Pyr modulesearch, Pyruvate oxidase and decarboxylase PP modulesearch Rossmann foldsearch, TPP-binding domainsearch, Single helix binsearch PF00205: Thiamine pyrophosphate enzyme, central domainsearch, PF02775: Thiamine pyrophosphate enzyme, C-terminal TPP binding domainsearch, PF02776: Thiamine pyrophosphate enzyme, N-terminal TPP binding domainsearch

Chain ID Molecular function (GO) Biological process (GO)
A, B, C, D (P27696) thiamine pyrophosphate bindingsearch acetolactate synthase activitysearch magnesium ion bindingsearch catalytic activitysearch transferase activitysearch metal ion bindingsearch butanediol metabolic processsearch

Chain InterPro annotation
A, B, C, D TPP-binding enzyme, conserved sitesearch Thiamine pyrophosphate enzyme, C-terminal TPP-bindingsearch Thiamine pyrophosphate enzyme, central domainsearch Thiamine pyrophosphate enzyme, N-terminal TPP-binding domainsearch Acetolactate synthase, catabolicsearch DHS-like NAD/FAD-binding domainsearch Thiamin diphosphate-binding foldsearch