Research workbench
Crystal structure of endoplasmic reticulum CA2+-ATPase (serca) from bovine muscle
Analyse Crystal structure of endoplasmic reticulum CA2+-ATPase (serca) from bovine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TLM
- Type
- protein
- Length
- 987 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SARCOPLASMIC/ENDOPLASMIC reticulum calcium ATPase 1
- EC
- 3.6.3.8
- UniProt
- Q0VCY0
- Ligands
- ACP, CA, MG, K
- Pockets
- 15 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SARCOPLASMIC/ENDOPLASMIC reticulum calcium ATPase 1 (EC 3.6.3.8) | protein | 987 | 44% helix, 16% strand | Q0VCY0 |
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
- K · Potassium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1165 | 0.84 | 0.85 | 109 | MG, ACP |
| 2 | 557 | 0.69 | 0.78 | 53 | empty |
| 3 | 290 | 0.60 | 0.79 | 28 | empty |
| 4 | 276 | 0.58 | 0.78 | 31 | empty |
| 5 | 181 | 0.56 | 0.79 | 20 | empty |
Compared structures
- 3TLM · Crystal Structure of Endoplasmic Reticulum Ca2+-ATPase (SERCA) From Bovine Muscle · the same entry in another collection · chain A against A, TM-score 1.00
- Q0VCY0 · AlphaFold monomer V2.0 prediction for SARCOPLASMIC/ENDOPLASMIC reticulum calcium ATPase 1… · 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 Q0VCY0
- Elsewhere: RCSB PDB 3TLM · PDBe 3TLM · UniProt Q0VCY0
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