Research workbench
Mamm ctd H264A-E289A-C267S
Analyse Mamm ctd H264A-E289A-C267S in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6G5E
- Type
- protein
- Length
- 82 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Magnetosome protein mamm
- UniProt
- Q6NE57
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Magnetosome protein mamm | protein | 82 | 40% helix, 35% strand | Q6NE57 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6G5E · MamM CTD H264A-E289A-C267S · 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 6G5E · PDBe 6G5E · UniProt Q6NE57
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