Research workbench
Structure of fission yeast RNA polymerase II ctd phosphatase FCP1- R271A bound to aluminum fluoride
Analyse Structure of fission yeast RNA polymerase II ctd phosphatase FCP1- R271A bound… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4XPZ
- Type
- protein
- Length
- 364 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
- AF3, MG
- Pockets
- 3 · best druggability 0.49
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 | 364 | 39% helix, 16% strand | Q9P376 |
Ligands and binding sites
- AF3 · Aluminum fluoride · ligand · chains A
- MG · Magnesium ion · metal · chains A
- PG4 · Tetraethylene glycol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 122 | 0.49 | 0.80 | 20 | empty |
| 2 | 75 | 0.40 | 0.79 | 23 | empty |
| 3 | 53 | 0.26 | 0.73 | 11 | empty |
Compared structures
- 4XPZ · Structure of fission yeast RNA polymerase II CTD phosphatase Fcp1-R271A bound to aluminum… · 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 0.98
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 4XPZ · PDBe 4XPZ · UniProt Q9P376
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