Research workbench
Structure of the transmembrane domain of the bacterial CNNM/CORC family MG2+ transporter in complex with MG2+
Analyse Structure of the transmembrane domain of the bacterial CNNM/CORC family MG2+… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7CFG
- Type
- protein
- Length
- 156 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemolysin
- UniProt
- A0A109QFA5
- Ligands
- ZN, MG
Structure
x-ray diffraction · 1 distinct chain · 87% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hemolysin | protein | 156 | 87% helix, 0% strand | A0A109QFA5 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
- MG · Magnesium ion · metal · chains A
- OLC · (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7CFG · Structure of the transmembrane domain of the bacterial CNNM/CorC family Mg2+ transporter… · 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 A0A109QFA5
- Elsewhere: RCSB PDB 7CFG · PDBe 7CFG · UniProt A0A109QFA5
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