Research workbench
Non-myristoylated bovine recoverin (truncated at C-terminus) with calcium bound to ef-hand 3
Analyse Non-myristoylated bovine recoverin (truncated at C-terminus) with calcium bound… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HET
- Type
- protein
- Length
- 728 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Recoverin
- UniProt
- P21457
- Ligands
- CA
- Pockets
- 16 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 59% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Recoverin | protein | 182 | 59% helix, 5% strand | P21457 |
Ligands and binding sites
- CA · Calcium ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 231 | 0.60 | 0.80 | 34 | empty |
| 2 | 215 | 0.59 | 0.80 | 32 | empty |
| 3 | 221 | 0.58 | 0.79 | 32 | empty |
| 4 | 204 | 0.57 | 0.80 | 31 | empty |
| 5 | 123 | 0.46 | 0.78 | 23 | empty |
Interfaces
4 interfaces between chains.
- A–B · 956 Ų buried · 11 hydrogen bonds · protein-protein
- C–D · 949 Ų buried · 12 hydrogen bonds · protein-protein
- A–D · 944 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 943 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 2HET · Non-myristoylated bovine recoverin (truncated at C-terminus) with calcium bound to… · the same entry in another collection · chain A against A, TM-score 1.00
- P21457 · AlphaFold monomer V2.0 prediction for recoverin (P21457) · a predicted model of the same protein · chain A against A, TM-score 0.92
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 P21457
- Elsewhere: RCSB PDB 2HET · PDBe 2HET · UniProt P21457
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