Research workbench
Cryoem structure of SERCA2B T1032STOP in E2-BEF3- state (CLASS2)
Analyse Cryoem structure of SERCA2B T1032STOP in E2-BEF3- state (CLASS2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LN9
- Type
- protein
- Length
- 987 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SARCOPLASMIC/ENDOPLASMIC reticulum calcium ATPase 2
- EC
- 7.2.2.10
- UniProt
- P16615
- Ligands
- BEF, MG
- Pockets
- 18 · best druggability 0.77
Structure
electron microscopy · 1 distinct chain · 44% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SARCOPLASMIC/ENDOPLASMIC reticulum calcium ATPase 2 (EC 7.2.2.10) | protein | 987 | 44% helix, 14% strand | P16615 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 852 | 0.77 | 0.80 | 66 | empty |
| 2 | 1183 | 0.76 | 0.79 | 78 | empty |
| 3 | 434 | 0.64 | 0.77 | 58 | empty |
| 4 | 416 | 0.60 | 0.75 | 36 | empty |
| 5 | 282 | 0.59 | 0.78 | 40 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 6LN9 · CryoEM structure of SERCA2b T1032stop in E2-BeF3- state (class2) · the same entry in another collection · chain A against A, TM-score 1.00
- P16615 · AlphaFold monomer V2.0 prediction for SARCOPLASMIC/ENDOPLASMIC reticulum calcium ATPase 2… · a predicted model of the same protein · chain A against A, TM-score 0.94
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 P16615
- Elsewhere: RCSB PDB 6LN9 · PDBe 6LN9 · UniProt P16615
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