Research workbench
Crystal structure of camkii-actinin complex bound to mes
Analyse Crystal structure of camkii-actinin complex bound to mes in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7B55
- Type
- protein
- Length
- 373 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P11798, P35609
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | — | protein | 308 | — | P11798 |
| A | — | protein | 65 | — | P35609 |
Ligands and binding sites
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7B55 · Crystal structure of CaMKII-actinin complex bound to MES · the same entry in another collection · chain B against B, TM-score 1.00
- P35609 · AlphaFold monomer V2.0 prediction for alpha-actinin-2 (P35609) · a predicted model of the same protein · chain A against A, TM-score 0.98
- P11798 · AlphaFold monomer V2.0 prediction for CALCIUM/CALMODULIN-dependent protein kinase type II… · a predicted model of the same protein · chain B against A, TM-score 0.97
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 P11798
- Every structure of UniProt P35609
- Elsewhere: RCSB PDB 7B55 · PDBe 7B55 · UniProt P11798 · UniProt P35609
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