› 1eg0

Electron Microscopy
11.5Å resolution

FITTING OF COMPONENTS WITH KNOWN STRUCTURE INTO AN 11.5 A CRYO-EM MAP OF THE E.COLI 70S RIBOSOME

Released:
DOI: 10.2210/pdb1eg0/pdb
PDB entry 1eg0 coloured by chain, front view.
PDB entry 1eg0 coloured by chain, side view.
PDB entry 1eg0 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Solution structure of the E. coli 70S ribosome at 11.5 A resolution.
Gabashvili IS, Agrawal RK, Spahn CM, Grassucci RA, Svergun DI, Frank J, Penczek P
Cell 100 537-49 (2000)
PMID: 10721991
Related structures: EMD-1003

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero pentadecamer (preferred)
PDBe Complex ID:
PDB-CPX-143901 (preferred)
Entry contents:
11 distinct polypeptide molecules
4 distinct RNA molecules
Macromolecules (15 distinct):
Small ribosomal subunit protein uS4 Chain: A
Molecule details ›
Chain: A
Length: 159 amino acids
Theoretical weight: 18.62 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P21466 (Residues: 43-200; Coverage: 79%)
Gene names: BSU29660, rpsD
Sequence domains:
Small ribosomal subunit protein uS5 Chain: B
Molecule details ›
Chain: B
Length: 148 amino acids
Theoretical weight: 15.69 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P21467 (Residues: 1-148; Coverage: 89%)
Gene names: BSU01330, rpsE, spcA
Sequence domains:
Small ribosomal subunit protein bS6 Chain: C
Small ribosomal subunit protein uS7 Chain: D
Small ribosomal subunit protein uS8 Chain: E
Small ribosomal subunit protein uS15 Chain: F
Small ribosomal subunit protein uS17 Chain: G
PROTEIN (S20 RIBOSOMAL PROTEIN) Chain: H
Large ribosomal subunit protein uL1 Chain: N
Large ribosomal subunit protein uL6 Chain: J
Large ribosomal subunit protein uL11 Chain: K
FRAGMENT OF 16S RRNA HELIX 23 Chain: I
FRAGMENT OF 23S RRNA Chain: L
HELIX 95 OF 23S RRNA Chain: M
FORMYL-METHIONYL-TRNA Chain: O

Ligands and Environments

No bound ligands
5 modified residues:
Ligand 4SU 1 x 4SU
Ligand H2U 1 x H2U
Ligand OMC 1 x OMC
Ligand 5MU 1 x 5MU
Ligand PSU 1 x PSU

Experiments and Validation Details

wwPDB Validation report is not available for this EM entry.
Resolution: 11.5Å
Relevant EMDB volumes: EMD-1003

Quick links

Citations

48 review citations

How cryo-EM is revolutionizing structural biology.
Bai et al. (2015)
47 more

2 mentions without citation

Evolving data standards for cryo-EM structures.
Lawson et al. (2020)
1 more