Research workbench
Structure of the kinase associated domain-1 (KA1) from KCC4P
Analyse Structure of the kinase associated domain-1 (KA1) from KCC4P in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OSM
- Type
- protein
- Length
- 119 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE-protein kinase KCC4
- EC
- 2.7.11.1
- UniProt
- P25389
- Ligands
- SRT
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE-protein kinase KCC4 (EC 2.7.11.1) | protein | 119 | 37% helix, 32% strand | P25389 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3OSM · Structure of the Kinase Associated Domain-1 (KA1) from Kcc4p · the same entry in another collection · chain A against A, TM-score 1.00
- P25389 · AlphaFold monomer V2.0 prediction for probable SERINE/THREONINE- protein kinase KCC4… · a predicted model of the same protein · chain A against A, TM-score 0.79
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 P25389
- Elsewhere: RCSB PDB 3OSM · PDBe 3OSM · UniProt P25389
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