MolNFT v1 · #155919 · protein
Cryoem structure of SERCA2B T1032STOP in E1-2CA2+-amppcp (CLASS3)
6LN7 · SARCOPLASMIC/ENDOPLASMIC reticulum calcium ATPase 2: “Cryoem structure of SERCA2B T1032STOP in E1-2CA2+-amppcp (CLASS3)”. Electron microscopy, 3 ligands (ACP, CA, MG), 13 pockets (best druggability 0.86). MolNFT v1 #155919 on…
- PDB
- 6LN7
- Type
- protein
- Length
- 1,011 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
- ACP, CA, MG
- Pockets
- 13 · best druggability 0.86
Structure
electron microscopy · 1 distinct chain · 47% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SARCOPLASMIC/ENDOPLASMIC reticulum calcium ATPase 2 (EC 7.2.2.10) | protein | 1011 | 47% helix, 16% strand | P16615 |
Ligands and binding sites
- ACP · Phosphomethylphosphonic acid adenylate ester · ligand · chains A
- CA · Calcium ion · metal · 2 copies · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 885 | 0.86 | 0.88 | 98 | ACP |
| 2 | 442 | 0.66 | 0.79 | 37 | empty |
| 3 | 296 | 0.66 | 0.81 | 37 | empty |
| 4 | 420 | 0.63 | 0.76 | 33 | empty |
| 5 | 231 | 0.55 | 0.78 | 26 | empty |
Compared structures
- 6LN7 · CryoEM structure of SERCA2b T1032stop in E1-2Ca2+-AMPPCP (class3) · 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 0.66
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 6LN7 · PDBe 6LN7 · UniProt P16615
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