Research workbench
Cu-metallothionein from saccharomyces cerevisiae, NMR, minimized average structure
Analyse Cu-metallothionein from saccharomyces cerevisiae, NMR, minimized average… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1AQR
- Type
- protein
- Length
- 40 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cu-metallothionein
- UniProt
- P07215
- Ligands
- CU1
Structure
solution nmr · 1 distinct chain · 8% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cu-metallothionein | protein | 40 | 8% helix, 0% strand | P07215 |
Ligands and binding sites
- CU1 · Copper (I) ion · metal · 7 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1AQR · Cu-metallothionein from saccharomyces cerevisiae, NMR, minimized average structure · the same entry in another collection · chain A against A, TM-score 1.00
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 P07215
- Elsewhere: RCSB PDB 1AQR · PDBe 1AQR · UniProt P07215
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