1d8t Summary



The structure was published by Heffron, S.E. and Jurnak, F., in 2000 in a paper entitled "Structure of an EF-TU Complex with a Thiazolyl Peptide Antibiotic Determined at 2.35 A Resolution: Atomic Basis for Ge2270A Inhibition of EF-TU." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.35 Å and deposited in 1999.

The experimental data on which the structure is based was not deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely ELONGATION FACTOR TU and THIOCILLIN GE2270.

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 ELONGATION FACTOR TU P0CE47 (2-394) (EFTU1_ECOLI)search Escherichia coli K-12search 99% 393 99%
B ELONGATION FACTOR TU P0CE47 (2-394) (EFTU1_ECOLI)search Escherichia coli K-12search 99% 393 99%
C THIOCILLIN GE2270 Q7M0J8 (1-14) (THCL_PLARO)search Planobispora roseasearch 100% 15 100%
D THIOCILLIN GE2270 Q7M0J8 (1-14) (THCL_PLARO)search Planobispora roseasearch 100% 15 100%

This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P0CE47 (2 - 394) ELONGATION FACTOR TU Escherichia coli
Q7M0J8 (1 - 14) THIOCILLIN GE2270 Planobispora rosea

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P0CE47) Elongation factorssearch, EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domainsearch, G proteinssearch P-loop containing nucleotide triphosphate hydrolasessearch, Translation factorssearch PF00009: Elongation factor Tu GTP binding domainsearch, PF03143: Elongation factor Tu C-terminal domainsearch, PF03144: Elongation factor Tu domain 2search
C, D (Q7M0J8)

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A, B (P0CE47) GTP bindingsearch translation elongation factor activitysearch GTPase activitysearch protein bindingsearch nucleotide bindingsearch intracellularsearch cytoplasmsearch membranesearch plasma membranesearch translational elongationsearch response to antibioticsearch GTP catabolic processsearch translationsearch
C, D (Q7M0J8) extracellular regionsearch defense response to bacteriumsearch cytolysissearch

Chain InterPro annotation
A, B Elongation factor, GTP-binding domainsearch Translation elongation factor EFTu/EF1A, C-terminalsearch Translation elongation factor EFTu/EF1A, domain 2search Translation elongation factor EFTu/EF1A, bacterial/organellesearch Small GTP-binding protein domainsearch Translation protein, beta-barrel domainsearch Translation elongation factor EF1A/initiation factor IF2gamma, C-terminalsearch P-loop containing nucleoside triphosphate hydrolasesearch
C, D