1e94 Summary

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PDB entry 1e94 (supersedes 1doo)

HSLV-HSLU FROM E.COLI

The structure was published by Song, H.K., Hartmann, C., Ravishankar, R., et al., Behrendt, R., Moroder, L., and Huber, R., in 2000 in a paper entitled "Mutational Studies on Hslu and its Docking Mode with Hslv" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.8 Å and deposited in 2000.

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

This PDB entry contains a complex of 2 biomacromolecules, namely HEAT SHOCK PROTEIN HSLV and HEAT SHOCK PROTEIN HSLU.

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 has more than one probable quaternary state observed. For more details see the quaternary structure page.

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 HEAT SHOCK PROTEIN HSLV P0A7B8 (2-176) (HSLV_ECOLI)search Escherichia coli K-12search 99% 175 99%
B HEAT SHOCK PROTEIN HSLV P0A7B8 (2-176) (HSLV_ECOLI)search Escherichia coli K-12search 99% 175 99%
C HEAT SHOCK PROTEIN HSLV P0A7B8 (2-176) (HSLV_ECOLI)search Escherichia coli K-12search 99% 175 99%
D HEAT SHOCK PROTEIN HSLV P0A7B8 (2-176) (HSLV_ECOLI)search Escherichia coli K-12search 99% 175 99%
E HEAT SHOCK PROTEIN HSLU P0A6H5 (2-443) (HSLU_ECOLI)search Escherichia coli K-12search 100% 449 91%
F HEAT SHOCK PROTEIN HSLU P0A6H5 (2-443) (HSLU_ECOLI)search Escherichia coli K-12search 100% 449 91%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P0A7B8 (2 - 176) HEAT SHOCK PROTEIN HSLV Escherichia coli BL21(DE3)
P0A6H5 (2 - 443) HEAT SHOCK PROTEIN HSLU Escherichia coli BL21(DE3)

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B, C, D (P0A7B8) Proteasome subunitssearch Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1search PF00227: Proteasome subunitsearch
E, F (P0A6H5) Extended AAA-ATPase domainsearch P-loop containing nucleotide triphosphate hydrolasessearch, DNA helicase RuvA subunit, C-terminal domainsearch, Helicase, Ruva Protein; domain 3search PF00004: ATPase family associated with various cellular activities (AAA)search, PF07724: AAA domain (Cdc48 subfamily)search, PF10431: C-terminal, D2-small domain, of ClpB proteinsearch

Chain ID Cellular component (GO) Molecular function (GO) Biological process (GO)
A, B, C, D (P0A7B8) proteasome core complexsearch HslUV protease complexsearch cytoplasmsearch cytosolsearch threonine-type endopeptidase activitysearch protein bindingsearch identical protein bindingsearch peptidase activitysearch hydrolase activitysearch metal ion bindingsearch catalytic activitysearch proteolysissearch proteolysis involved in cellular protein catabolic processsearch response to heatsearch protein catabolic processsearch response to stresssearch metabolic processsearch
E, F (P0A6H5) cytoplasmsearch HslUV protease complexsearch membranesearch identical protein bindingsearch ATP bindingsearch protein bindingsearch nucleotide bindingsearch ATPase activitysearch peptidase activity, acting on L-amino acid peptidessearch nucleoside-triphosphatase activitysearch ATP catabolic processsearch proteolysissearch protein unfoldingsearch response to heatsearch response to stresssearch

Chain InterPro annotation
A, B, C, D Proteasome, subunit alpha/betasearch ATP-dependent protease, HslV subunitsearch Proteasome B-type subunitsearch Nucleophile aminohydrolases, N-terminalsearch
E, F AAA+ ATPase domainsearch ATPase, AAA-type, coresearch Heat shock protein HslUsearch Clp ATPase, C-terminalsearch P-loop containing nucleoside triphosphate hydrolasesearch