Research workbench
Serine 16 phosphorylated phospholamban pentamer, hybrid solution and solid-state NMR structural ensemble
Analyse Serine 16 phosphorylated phospholamban pentamer, hybrid solution and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2M3B
- Type
- protein
- Length
- 260 residues
- Chains
- 5
- Method
- solution nmr; solid-state nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cardiac phospholamban
- UniProt
- P61015
- Pockets
- 2 · best druggability 0.75
Structure
solution nmr; solid-state nmr · 1 distinct chain · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | Cardiac phospholamban | protein | 52 | 79% helix, 0% strand | P61015 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 269 | 0.75 | 0.87 | 25 | empty |
| 2 | 88 | 0.34 | 0.74 | 16 | empty |
Interfaces
10 interfaces between chains.
- A–B · 791 Ų buried · 20 hydrogen bonds · protein-protein
- C–D · 783 Ų buried · 20 hydrogen bonds · protein-protein
- A–E · 782 Ų buried · 20 hydrogen bonds · protein-protein
- B–C · 778 Ų buried · 20 hydrogen bonds · protein-protein
- D–E · 771 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 modified (phosphorylation).
Compared structures
- 2M3B · Serine 16 phosphorylated phospholamban pentamer, Hybrid solution and solid-state NMR… · the same entry in another collection · chain A against A, TM-score 1.00
- P61015 · AlphaFold monomer V2.0 prediction for cardiac phospholamban (P61015) · a predicted model of the same protein · chain A against A, TM-score 0.50
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 P61015
- Elsewhere: RCSB PDB 2M3B · PDBe 2M3B · UniProt P61015
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