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Solution structure of the rgs domain from human regulator of G-protein signaling 12 (RGS12)
Analyse Solution structure of the rgs domain from human regulator of G-protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2EBZ
- Type
- protein
- Length
- 155 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Regulator of G-protein signaling 12
- UniProt
- O14924
- Pockets
- 1 · best druggability 0.36
Structure
solution nmr · 1 distinct chain · 63% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Regulator of G-protein signaling 12 | protein | 155 | 63% helix, 0% strand | O14924 |
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 | 14 | empty |
Compared structures
- 2EBZ · Solution structure of the RGS domain from human Regulator of G-protein signaling 12… · the same entry in another collection · chain A against A, TM-score 1.00
- O14924 · AlphaFold monomer V2.0 prediction for regulator of G-protein signaling 12 (O14924) · a predicted model of the same protein · chain A against A, TM-score 0.89
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 O14924
- Elsewhere: RCSB PDB 2EBZ · PDBe 2EBZ · UniProt O14924
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