› 7nmr

X-ray diffraction
1.15Å resolution

Crystal structure of beta-2-microglobulin D76S mutant

Released:
DOI: 10.2210/pdb7nmr/pdb
PDB entry 7nmr coloured by chain, front view.
PDB entry 7nmr coloured by chain, side view.
PDB entry 7nmr coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The effect of mutation on an aggregation-prone protein: An in vivo, in vitro, and in silico analysis.
Guthertz N, van der Kant R, Martinez RM, Xu Y, Trinh C, Iorga BI, Rousseau F, Schymkowitz J, Brockwell DJ, Radford SE
Proc Natl Acad Sci U S A 119 e2200468119 (2022)
PMID: 35613051

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158314 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-2-microglobulin Chain: AAA
Molecule details ›
Chain: AAA
Length: 98 amino acids
Theoretical weight: 11.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P61769 (Residues: 21-117; Coverage: 98%)
Gene names: B2M, CDABP0092, HDCMA22P
Sequence domains: Immunoglobulin C1-set domain

Ligands and Environments

1 bound ligand:
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE MASSIF-1
Unit cell:
a: 53.339Å b: 28.795Å c: 63.004Å
α: 90° β: 96.93° γ: 90°
R-values:
R R work R free
0.15 0.148 0.182
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Mechanisms and pathology of protein misfolding and aggregation.
Louros et al. (2023)
2 other articles

1 mention without citation

The effect of mutation on an aggregation-prone protein: An in vivo, in vitro, and in silico analysis.
Guthertz et al. (2022)