› 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
OpenAccess logo 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)
3 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)