Research workbench
Calcium-saturated GCAMP2 dimer
Analyse Calcium-saturated GCAMP2 dimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EK7
- Type
- protein
- Length
- 389 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myosin light chain kinase, green fluorescent protein, calmodulin chimera
- UniProt
- P42212, P0DP29
- Ligands
- CRO, CA
- Pockets
- 3 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myosin light chain kinase, green fluorescent protein, calmodulin chimera | protein | 389 | 34% helix, 32% strand | P42212, P0DP29 |
Ligands and binding sites
- CRO · {2-[(1R,2R)-1-amino-2-hydroxypropyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl}acetic acid · ligand · chains A
- CA · Calcium ion · metal · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 659 | 0.67 | 0.75 | 45 | empty |
| 2 | 280 | 0.66 | 0.82 | 35 | CRO |
| 3 | 79 | 0.35 | 0.76 | 21 | empty |
Modifications
Observed in the structure: 2 cofactor (chromophore).
Compared structures
- 3EK7 · Calcium-saturated GCaMP2 dimer · the same entry in another collection · chain A against A, TM-score 1.00
- P42212 · AlphaFold monomer V2.0 prediction for green fluorescent protein (P42212) · a predicted model of the same protein · chain A against A, TM-score 0.37
- P0DP29 · AlphaFold monomer V2.0 prediction for calmodulin-1 (P0DP29) · a predicted model of the same protein · chain A against A, TM-score 0.20
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 P42212
- Every structure of UniProt P0DP29
- Elsewhere: RCSB PDB 3EK7 · PDBe 3EK7 · UniProt P42212 · UniProt P0DP29
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