Research workbench
Structure of human PAF1 and LEO1 complex
Analyse Structure of human PAF1 and LEO1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4M6T
- Type
- protein
- Length
- 177 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA polymerase II-associated factor 1 homolog, linker, RNA polymerase-associated protein…
- UniProt
- Q8N7H5, Q8WVC0
- Ligands
- SAM
- Pockets
- 2 · best druggability 0.47
Structure
x-ray diffraction · 1 distinct chain · 18% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA polymerase II-associated factor 1 homolog, linker, RNA polymerase-associated protein LEO1 | protein | 177 | 18% helix, 32% strand | Q8N7H5, Q8WVC0 |
Ligands and binding sites
- SAM · S-adenosylmethionine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 100 | 0.47 | 0.79 | 22 | empty |
| 2 | 72 | 0.33 | 0.75 | 13 | empty |
Compared structures
- 4M6T · Structure of human Paf1 and Leo1 complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q8WVC0 · AlphaFold monomer V2.0 prediction for RNA polymerase-associated protein LEO1 (Q8WVC0) · a predicted model of the same protein · chain A against A, TM-score 0.47
- Q8N7H5 · AlphaFold monomer V2.0 prediction for RNA polymerase II-associated factor 1 homolog… · a predicted model of the same protein · chain A against A, TM-score 0.33
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 Q8N7H5
- Every structure of UniProt Q8WVC0
- Elsewhere: RCSB PDB 4M6T · PDBe 4M6T · UniProt Q8N7H5 · UniProt Q8WVC0
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