Research workbench
MamM CTD H264E - Zinc form 1
Analyse MamM CTD H264E - Zinc form 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6H5M
- Type
- protein
- Length
- 89 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.6
- Source
- Magnetospirillum gryphiswaldense
- Molecule
- Magnetosome protein MamM, Cation efflux protein family
- UniProt
- Q6NE57
- Ligands
- ZN
Structure
x-ray diffraction · resolution 1.6 · 1 distinct chain · 35% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Magnetosome protein MamM, Cation efflux protein family | protein | 89 | 35% helix, 33% strand | Q6NE57 |
Ligands and binding sites
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
- 6H5M · Mamm ctd H264E - zinc form 1 · 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 6H5M · PDBe 6H5M · UniProt Q6NE57
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