Research workbench
Crystal structure of coactivator-associated arginine methyltransferase 1 with methylenesinefungin
Analyse Crystal structure of coactivator-associated arginine methyltransferase 1 with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4IKP
- Type
- protein
- Length
- 1,340 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q86X55
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D | — | protein | 335 | — | Q86X55 |
| B | — | protein | 335 | — | Q86X55 |
Compared structures
- 4IKP · Crystal structure of coactivator-associated arginine methyltransferase 1 with… · the same entry in another collection · chain D against D, TM-score 1.00
- Q86X55 · AlphaFold monomer V2.0 prediction for histone-arginine methyltransferase CARM1 (Q86X55) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q86X55
- Elsewhere: RCSB PDB 4IKP · PDBe 4IKP · UniProt Q86X55
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