Research workbench
Calcium-free GCAMP2 (calcium binding deficient mutant)
Analyse Calcium-free GCAMP2 (calcium binding deficient mutant) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EKJ
- Type
- protein
- Length
- 301 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
- Pockets
- 2 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 20% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myosin light chain kinase, green fluorescent protein, calmodulin chimera | protein | 301 | 20% helix, 41% 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
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 391 | 0.77 | 0.86 | 57 | CRO |
| 2 | 158 | 0.48 | 0.77 | 29 | empty |
Modifications
Observed in the structure: 2 cofactor (chromophore).
Compared structures
- 3EKJ · Calcium-free GCaMP2 (calcium binding deficient mutant) · 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 0.48
- P0DP29 · AlphaFold monomer V2.0 prediction for calmodulin-1 (P0DP29) · a predicted model of the same protein · chain A against A, TM-score 0.24
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 3EKJ · PDBe 3EKJ · UniProt P42212 · UniProt P0DP29
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