Research workbench
Crystal structure of the bateman domain of murine magnesium transporter CNNM2 bound to AMP
Analyse Crystal structure of the bateman domain of murine magnesium transporter CNNM2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4P1G
- Type
- protein
- Length
- 152 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Metal transporter CNNM2
- UniProt
- Q3TWN3
- Ligands
- AMP
- Pockets
- 1 · best druggability 0.36
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Metal transporter CNNM2 | protein | 152 | 39% helix, 27% strand | Q3TWN3 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · chains A
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 | 58 | 0.36 | 0.79 | 13 | AMP |
Compared structures
- 4P1G · Crystal structure of the Bateman domain of murine magnesium transporter CNNM2 bound to AMP · the same entry in another collection · chain A against A, TM-score 1.00
- Q3TWN3 · AlphaFold monomer V2.0 prediction for metal transporter CNNM2 (Q3TWN3) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q3TWN3
- Elsewhere: RCSB PDB 4P1G · PDBe 4P1G · UniProt Q3TWN3
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