Research workbench
MamM CTD H264E-E289H
Analyse MamM CTD H264E-E289H in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HAN
- Type
- protein
- Length
- 355 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.6
- Source
- Magnetospirillum gryphiswaldense
- Molecule
- Magnetosome protein MamM, Cation efflux protein family
- UniProt
- Q6NE57
- Ligands
- SO4, CL
- Pockets
- 1 · best druggability 0.78
Structure
x-ray diffraction · resolution 2.6 · 4 distinct chains · 36% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Magnetosome protein MamM, Cation efflux protein family | protein | 94 | 33% helix, 33% strand | Q6NE57 |
| B | Magnetosome protein MamM, Cation efflux protein family | protein | 84 | 39% helix, 36% strand | Q6NE57 |
| C | Magnetosome protein MamM, Cation efflux protein family | protein | 95 | 32% helix, 34% strand | Q6NE57 |
| D | Magnetosome protein MamM, Cation efflux protein family | protein | 82 | 41% helix, 37% strand | Q6NE57 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A, B, C, D
- CL · Chloride ion · ion · chains A
- BME · Beta-mercaptoethanol · additive · 4 copies · chains B, A, C, D
- 1PE · Pentaethylene glycol · additive · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1115 | 0.78 | 0.80 | 91 | 1PE, BME |
Interfaces
5 interfaces between chains.
- A–C · 591 Ų buried · 14 hydrogen bonds · protein-protein
- A–D · 541 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 516 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 333 Ų buried · 7 hydrogen bonds · protein-protein
- C–D · 297 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (additive adduct).
Compared structures
- 6HAN · Mamm ctd H264E-E289H · 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 6HAN · PDBe 6HAN · UniProt Q6NE57
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