› 1qjl

Solution NMR

METALLOTHIONEIN MTA FROM SEA URCHIN (BETA DOMAIN)

Released:
DOI: 10.2210/pdb1qjl/pdb
PDB entry 1qjl coloured by chain, front view.
PDB entry 1qjl coloured by chain, side view.
PDB entry 1qjl coloured by chain, top view.
Source organism: Strongylocentrotus purpuratus
Primary publication:
NMR structure of the sea urchin (Strongylocentrotus purpuratus) metallothionein MTA.
Riek R, Prêcheur B, Wang Y, Mackay EA, Wider G, Güntert P, Liu A, Kägi JH, Wüthrich K
J Mol Biol 291 417-28 (1999)
PMID: 10438629

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138160 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Metallothionein-A Chain: A
Molecule details ›
Chain: A
Length: 28 amino acids
Theoretical weight: 2.68 KDa
Source organism: Strongylocentrotus purpuratus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P04734 (Residues: 37-64; Coverage: 44%)
Gene name: MTA
Sequence domains: Metallothionein

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

11 review citations

Advances in the structure and chemistry of metallothioneins.
Romero-Isart et al. (2002)
10 more

1 mention without citation

The sea urchin metallothionein system: Comparative evaluation of the SpMTA and SpMTB metal-binding preferences.
Tomas et al. (2013)