Research workbench
Structure of the cbs domain of the bacterial CNNM/CORC family MG2+ transporter in complex with ATP
Analyse Structure of the cbs domain of the bacterial CNNM/CORC family MG2+ transporter… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7CFI
- Type
- protein
- Length
- 142 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemolysin
- UniProt
- A0A109QFA5
- Ligands
- ATP, MG
- Pockets
- 1 · best druggability 0.38
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hemolysin | protein | 142 | 44% helix, 24% strand | A0A109QFA5 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 70 | 0.38 | 0.78 | 15 | ATP |
Compared structures
- 7CFI · Structure of the CBS domain of the bacterial CNNM/CorC family Mg2+ transporter in complex… · 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 7CFI · PDBe 7CFI · UniProt A0A109QFA5
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