Research workbench
Solution structure of sole a-domain of human metallothionein-3 (mt-3)
Analyse Solution structure of sole a-domain of human metallothionein-3 (mt-3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FJ5
- Type
- protein
- Length
- 37 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Metallothionein-3
- UniProt
- P25713
- Ligands
- CD
Structure
solution nmr · 1 distinct chain · 16% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Metallothionein-3 | protein | 37 | 16% helix, 0% strand | P25713 |
Ligands and binding sites
- CD · Cadmium ion · metal · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P25713
- Elsewhere: RCSB PDB 2FJ5 · PDBe 2FJ5 · UniProt P25713
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