MolNFT v1 · #150842 · protein
Mamm ctd H264E - zinc form 2
6H5U · Magnetosome protein mamm, cation efflux protein family: “Mamm ctd H264E - zinc form 2”. X-ray diffraction, 2 ligands (ZN, SO4), 2 pockets (best druggability 0.57). MolNFT v1 #150842 on GenesisL1: 3D structure, binding sites and…
- PDB
- 6H5U
- Type
- protein
- Length
- 271 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Magnetosome protein mamm, cation efflux protein family
- UniProt
- Q6NE57
- Ligands
- ZN, SO4
- Pockets
- 2 · best druggability 0.57
Structure
x-ray diffraction · 4 distinct chains · 36% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Magnetosome protein mamm, cation efflux protein family | protein | 90 | 36% helix, 32% strand | Q6NE57 |
| B | Magnetosome protein mamm, cation efflux protein family | protein | 91 | 35% helix, 32% strand | Q6NE57 |
| C | Magnetosome protein mamm, cation efflux protein family | protein | 82 | 40% helix, 35% strand | Q6NE57 |
| H | Magnetosome protein mamm, cation efflux protein family | protein | 8 | 0% helix, 0% strand | Q6NE57 |
Ligands and binding sites
- ZN · Zinc ion · metal · 3 copies · chains A, C
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
- BME · Beta-mercaptoethanol · additive · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 376 | 0.57 | 0.75 | 34 | empty |
| 2 | 195 | 0.57 | 0.80 | 26 | BME |
Interfaces
4 interfaces between chains.
- B–H · 346 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 194 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 192 Ų buried · 0 hydrogen bonds · protein-protein
- C–H · 48 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 covalent (additive adduct).
Compared structures
- 6H5U · MamM CTD H264E - Zinc form 2 · 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 6H5U · PDBe 6H5U · UniProt Q6NE57
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