MolNFT v1 · #32966 · protein + DNA
Crystal structure of the human transcription cofactor PC4 in complex with single-stranded DNA
2C62 · Activated RNA polymerase II transcriptional coactivator P15: “Crystal structure of the human transcription cofactor PC4 in complex with single-stranded DNA”. X-ray diffraction, 1 ligand (SO4), 1 pocket (best druggability 0.58).…
- PDB
- 2C62
- Type
- protein + DNA
- Length
- 148 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Activated RNA polymerase II transcriptional coactivator P15…
- UniProt
- P53999
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.58
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Activated RNA polymerase II transcriptional coactivator P15 | protein | 66 | 27% helix, 52% strand | P53999 |
| C | 5'-D(*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP *TP*TP*TP*TP*TP*TP*TP*TP*TP*G)-3' | dna | 16 | — | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 164 | 0.58 | 0.82 | 20 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1477 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 878 Ų buried · 18 hydrogen bonds · protein-nucleic
- A–C · 745 Ų buried · 14 hydrogen bonds · protein-nucleic
Compared structures
- 2C62 · Crystal Structure of the Human Transcription Cofactor PC4 in Complex with Single-Stranded… · the same entry in another collection · chain A against A, TM-score 1.00
- P53999 · AlphaFold monomer V2.0 prediction for activated RNA polymerase II transcriptional… · a predicted model of the same protein · chain A against A, TM-score 0.93
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 P53999
- Elsewhere: RCSB PDB 2C62 · PDBe 2C62 · UniProt P53999
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