› 6lms

Solution NMR

Solution NMR structure cold shock domain of YB1 from Homo sapiens

Released:
DOI: 10.2210/pdb6lms/pdb
PDB entry 6lms coloured by chain, ensemble of 20 models, front view.
PDB entry 6lms coloured by chain, ensemble of 20 models, side view.
PDB entry 6lms coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of DNA binding to human YB-1 cold shock domain regulated by phosphorylation.
Zhang J, Fan JS, Li S, Yang Y, Sun P, Zhu Q, Wang J, Jiang B, Yang D, Liu M
OpenAccess logo Nucleic Acids Res 48 9361-9371 (2020)
PMID: 32710623

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-549745 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Y-box-binding protein 1 Chain: A
Molecule details ›
Chain: A
Length: 106 amino acids
Theoretical weight: 11.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P67809 (Residues: 51-140; Coverage: 28%)
Gene names: NSEP1, YB1, YBX1
Sequence domains: 'Cold-shock' DNA-binding domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 76%
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

A comprehensive review of the functions of YB-1 in cancer stemness, metastasis and drug resistance.
Alkrekshi et al. (2021)
4 more

1 mention without citation

Structural basis of DNA binding to human YB-1 cold shock domain regulated by phosphorylation.
Zhang et al. (2020)