Brand  (β version)

PDB ID: 3S04

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Ligands
Code Name Style Show Link
02U 14-methylhexadec-9-enoic acid PoSSuM
RAM Alpha-L-rhamnopyranose PoSSuM
Non-standard Residues
Code Name Show
DSE N-methyl-D-serine
DAL D-alanine
02V (2s)-(3,4-dihydroxyphenyl)(methylamino)ethanoic acid
Glycosylation
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Structure summary

Code : 3S04   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/ANTIBIOTIC
Title : Crystal structure of Escherichia coli type I signal peptidase in complex with an Arylomycin Lipoglycopeptide Antibiotic
Release Data : 2011-10-05
Compound :
mol_id molecule chains synonym
1 Signal peptidase I A,B SPase I, Leader peptidase I
ec: 3.4.21.89
fragment: Periplasmic domain, UNP residues 76-323
mol_id molecule chains
2 Glyco-Arylomycin I,J
Source :
mol_id organism_scientific expression_system
1 Escherichia coli  (taxid:83333) Escherichia coli  (taxid:469008)
strain: K12
gene: b2568, JW2552, lepB
expression_system_strain: BL21 (DE3)
expression_system_vector_type: PLASMID
expression_system_plasmid: pET3d
mol_id organism_scientific
2 Streptomyces sp.  (taxid:1931)
Authors : Paetzel, M., Luo, C.
Keywords : mostly-beta fold, Membrane bound, serine protease, Secreted preproteins, Cytoplasmic membrane, HYDROLASE-ANTIBIOTIC complex, signal peptidase, leader peptidase, signal peptide, leader peptide, serine-lysine dyad
Exp. method : X-RAY DIFFRACTION ( 2.44 Å )
Citation :

Synthesis and characterization of the arylomycin lipoglycopeptide antibiotics and the crystallographic analysis of their complex with signal peptidase.

Liu, J.,Luo, C.,Smith, P.A.  et al.
(2011)  J.Am.Chem.Soc.  133 : 17869 - 17877

PubMed: 21999324
DOI: 10.1021/ja207318n

Reaction

Chain : A, B
UniProt : P00803 (LEP_ECOLI)
Reaction: EC: Evidence:
Physiological Direction:
Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins. 3.4.21.89 -
-