Research workbench
MamM CTD H264E-E289H - Cadmium form
Analyse MamM CTD H264E-E289H - Cadmium form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6H85
- Type
- protein
- Length
- 81 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2
- Source
- Magnetospirillum gryphiswaldense
- Molecule
- Magnetosome protein MamM, Cation efflux protein family
- UniProt
- Q6NE57
- Ligands
- CD, SO4
Structure
x-ray diffraction · resolution 2 · 1 distinct chain · 40% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Magnetosome protein MamM, Cation efflux protein family | protein | 81 | 40% helix, 36% strand | Q6NE57 |
Ligands and binding sites
- CD · Cadmium ion · metal · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
- BME · Beta-mercaptoethanol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 covalent (additive adduct).
Compared structures
- 6H85 · Mamm ctd H264E-E289H - cadmium form · 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 Q6NE57
- Elsewhere: RCSB PDB 6H85 · PDBe 6H85 · UniProt Q6NE57
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