Research workbench
RNA polymerase II strand separated elongation complex
Analyse RNA polymerase II strand separated elongation complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SFO
- Type
- protein + DNA + RNA
- Length
- 3,566 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA strand; DNA strand; DNA-directed RNA polymerase II largest subunit; DNA-directed RNA…
- EC
- 2.7.7.6
- UniProt
- P04050, P08518, P16370, P20434, P20435, P20436, P27999, P22139, P38902, P40422
- Ligands
- ZN, MG
- Pockets
- 20 · best druggability 0.88
Structure
x-ray diffraction · 12 distinct chains · 30% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| R | RNA strand | rna | 10 | — | — |
| T | DNA strand | dna | 14 | — | — |
| A | DNA-directed RNA polymerase II largest subunit (EC 2.7.7.6) | protein | 1395 | 37% helix, 13% strand | P04050 |
| B | DNA-directed RNA polymerase II 140 kda polypeptide (EC 2.7.7.6) | protein | 1106 | 27% helix, 20% strand | P08518 |
| C | DNA-directed RNA polymerase II 45 kda polypeptide (EC 2.7.7.6) | protein | 266 | 27% helix, 23% strand | P16370 |
| E | DNA-directed RNA polymerases I, II, and III 27 kda polypeptide (EC 2.7.7.6) | protein | 214 | 35% helix, 16% strand | P20434 |
| F | DNA-directed RNA polymerases I, II, and III 23 kda polypeptide (EC 2.7.7.6) | protein | 84 | 29% helix, 14% strand | P20435 |
| H | DNA-directed RNA polymerases I, II, and III 14.5 kda polypeptide (EC 2.7.7.6) | protein | 133 | 0% helix, 44% strand | P20436 |
| I | DNA-directed RNA polymerase II 14.2 kda polypeptide (EC 2.7.7.6) | protein | 119 | 3% helix, 19% strand | P27999 |
| J | DNA-directed RNA polymerases I, II, and III 8.3 kda polypeptide (EC 2.7.7.6) | protein | 65 | 42% helix, 0% strand | P22139 |
| K | DNA-directed RNA polymerase II 13.6 kda polypeptide (EC 2.7.7.6) | protein | 114 | 36% helix, 24% strand | P38902 |
| L | DNA-directed RNA polymerases I, II, and III 7.7 kda polypeptide (EC 2.7.7.6) | protein | 46 | 0% helix, 11% strand | P40422 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1102 | 0.88 | 0.90 | 122 | empty |
| 2 | 605 | 0.85 | 0.90 | 66 | empty |
| 3 | 992 | 0.81 | 0.83 | 79 | empty |
| 4 | 672 | 0.80 | 0.85 | 64 | empty |
| 5 | 187 | 0.80 | 0.95 | 36 | empty |
Interfaces
27 interfaces between chains.
- A–B · 9760 Ų buried · 126 hydrogen bonds · protein-protein
- A–E · 2191 Ų buried · 30 hydrogen bonds · protein-protein
- C–K · 2130 Ų buried · 16 hydrogen bonds · protein-protein
- B–C · 1767 Ų buried · 36 hydrogen bonds · protein-protein
- A–F · 1739 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 1SFO · RNA polymerase II strand separated elongation complex · the same entry in another collection · chain R against R, 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 P04050
- Every structure of UniProt P08518
- Every structure of UniProt P16370
- Every structure of UniProt P20434
- Every structure of UniProt P20435
- Every structure of UniProt P20436
- Every structure of UniProt P27999
- Every structure of UniProt P22139
- Every structure of UniProt P38902
- Every structure of UniProt P40422
- Elsewhere: RCSB PDB 1SFO · PDBe 1SFO · UniProt P04050 · UniProt P08518 · UniProt P16370 · UniProt P20434 · UniProt P20435 · UniProt P20436 · UniProt P27999 · UniProt P22139 · UniProt P38902 · UniProt P40422
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