MolNFT v1 · #146337 · protein
Structure of DSE3-CSM1 complex
6DEI: “Structure of DSE3-CSM1 complex”. X-ray diffraction. MolNFT v1 #146337 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6DEI
- Type
- protein
- Length
- 253 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P25651, Q08729
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 107 | — | P25651 |
| B | — | protein | 105 | — | P25651 |
| C | — | protein | 24 | — | Q08729 |
| D | — | protein | 17 | — | Q08729 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6DEI · Structure of Dse3-Csm1 complex · the same entry in another collection · chain D against D, TM-score 1.00
- P25651 · AlphaFold monomer V2.0 prediction for monopolin complex subunit CSM1 (P25651) · a predicted model of the same protein · chain A against A, TM-score 0.93
- Q08729 · AlphaFold monomer V2.0 prediction for protein DSE3 (Q08729) · a predicted model of the same protein · chain D against A, TM-score 0.32
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 P25651
- Every structure of UniProt Q08729
- Elsewhere: RCSB PDB 6DEI · PDBe 6DEI · UniProt P25651 · UniProt Q08729
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