› 1qb2

X-ray diffraction
2.1Å resolution

CRYSTAL STRUCTURE OF THE CONSERVED SUBDOMAIN OF HUMAN PROTEIN SRP54M AT 2.1A RESOLUTION: EVIDENCE FOR THE MECHANISM OF SIGNAL PEPTIDE BINDING

Released:
DOI: 10.2210/pdb1qb2/pdb
PDB entry 1qb2 coloured by chain, front view.
PDB entry 1qb2 coloured by chain, side view.
PDB entry 1qb2 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the conserved subdomain of human protein SRP54M at 2.1 A resolution: evidence for the mechanism of signal peptide binding.
Clemons WM, Gowda K, Black SD, Zwieb C, Ramakrishnan V
J Mol Biol 292 697-705 (1999)
PMID: 10497032

Function and Biology Details

Reaction catalysed: 
GTP + H(2)O = GDP + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158174 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Signal recognition particle subunit SRP54 Chains: A, B
Molecule details ›
Chains: A, B
Length: 109 amino acids
Theoretical weight: 12.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P61011 (Residues: 326-434; Coverage: 22%)
Gene name: SRP54
Sequence domains: Signal peptide binding domain
Structure domains: Signal recognition particle, SRP54 subunit, M-domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C, NSLS BEAMLINE X25
Spacegroup: P212121
Unit cell:
a: 28.91Å b: 61.34Å c: 129.22Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.245 0.245 0.318
Expression system: Escherichia coli

Quick links

Citations

10 review citations

The signal recognition particle.
Keenan et al. (2001)
9 more

7 mentions without citation

Recognition and Degradation of Mislocalized Proteins in Health and Disease.
Hegde et al. (2019)
6 more