Research workbench
The structure of FCP1, an essential RNA polymerase II ctd phosphatase
Analyse The structure of FCP1, an essential RNA polymerase II ctd phosphatase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EF1
- Type
- protein
- Length
- 372 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA polymerase II subunit a C-terminal domain phosphatase
- EC
- 3.1.3.16
- UniProt
- Q9P376
- Ligands
- MG
- Pockets
- 4 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA polymerase II subunit a C-terminal domain phosphatase (EC 3.1.3.16) | protein | 372 | 39% helix, 16% strand | Q9P376 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 76 | 0.54 | 0.86 | 20 | empty |
| 2 | 83 | 0.42 | 0.79 | 24 | empty |
| 3 | 91 | 0.36 | 0.75 | 18 | empty |
| 4 | 52 | 0.26 | 0.73 | 15 | empty |
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
- 3EF1 · The Structure of Fcp1, an essential RNA polymerase II CTD phosphatase · the same entry in another collection · chain A against A, TM-score 1.00
- Q9P376 · AlphaFold monomer V2.0 prediction for RNA polymerase II subunit a C-terminal domain… · a predicted model of the same protein · chain A against A, TM-score 0.96
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 Q9P376
- Elsewhere: RCSB PDB 3EF1 · PDBe 3EF1 · UniProt Q9P376
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