Research workbench
Crystal structure of the serine phosphatase of RNA polymerase II ctd (SSU72 superfamily) from drosophila melanogaster. orthorhombic crystal form. northeast structural genomics consortium target FR253.
Analyse Crystal structure of the serine phosphatase of RNA polymerase II ctd (SSU72… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FDF
- Type
- protein
- Length
- 764 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FR253
- UniProt
- Q9VWE4
- Pockets
- 11 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | FR253 | protein | 191 | 43% helix, 18% strand | Q9VWE4 |
Pockets
11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 828 | 0.77 | 0.81 | 57 | empty |
| 2 | 207 | 0.57 | 0.80 | 28 | empty |
| 3 | 211 | 0.52 | 0.77 | 40 | empty |
| 4 | 120 | 0.45 | 0.78 | 20 | empty |
| 5 | 64 | 0.43 | 0.82 | 15 | empty |
Interfaces
5 interfaces between chains.
- A–B · 504 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 365 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 274 Ų buried · 4 hydrogen bonds · protein-protein
- B–D · 69 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 19 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 44 modified (engineered).
Compared structures
- 3FDF · Crystal structure of the serine phosphatase of RNA polymerase II CTD (SSU72 superfamily)… · the same entry in another collection · chain A against A, TM-score 1.00
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 Q9VWE4
- Elsewhere: RCSB PDB 3FDF · PDBe 3FDF · UniProt Q9VWE4
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