Research workbench
Crystal structure of the human CDK12-cyclin K complex bound to amppnp
Analyse Crystal structure of the human CDK12-cyclin K complex bound to amppnp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CXA
- Type
- protein
- Length
- 1,148 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9NYV4, O75909
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 330 | — | Q9NYV4 |
| B | — | protein | 246 | — | O75909 |
| C | — | protein | 331 | — | Q9NYV4 |
| D | — | protein | 241 | — | O75909 |
Compared structures
- 4CXA · Crystal structure of the human CDK12-cyclin K complex bound to AMPPNP · the same entry in another collection · chain D against D, TM-score 1.00
- Q9NYV4 · AlphaFold monomer V2.0 prediction for cyclin-dependent kinase 12 (Q9NYV4) · a predicted model of the same protein · chain A against A, TM-score 0.98
- O75909 · AlphaFold monomer V2.0 prediction for cyclin-K (O75909) · a predicted model of the same protein · chain D 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 Q9NYV4
- Every structure of UniProt O75909
- Elsewhere: RCSB PDB 4CXA · PDBe 4CXA · UniProt Q9NYV4 · UniProt O75909
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