Research workbench
Crystal structure CBK1(NTR)-MOB2 complex
Analyse Crystal structure CBK1(NTR)-MOB2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NCM
- Type
- protein
- Length
- 273 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P43563, P53894
- Ligands
- ZN
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 183 | — | P43563 |
| B | — | protein | 90 | — | P53894 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5NCM · Crystal structure Cbk1(NTR)-Mob2 complex · the same entry in another collection · chain A against A, TM-score 1.00
- P43563 · AlphaFold monomer V2.0 prediction for CBK1 kinase activator protein MOB2 (P43563) · a predicted model of the same protein · chain A against A, TM-score 0.96
- P53894 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase CBK1 (P53894) · a predicted model of the same protein · chain B against A, TM-score 0.87
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 P43563
- Every structure of UniProt P53894
- Elsewhere: RCSB PDB 5NCM · PDBe 5NCM · UniProt P43563 · UniProt P53894
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