MolNFT v1 · #66391 · protein + DNA + RNA
Complete RNA polymerase II elongation complex VI
3HOY · DNA-directed RNA polymerase II subunit RPB1: “Complete RNA polymerase II elongation complex VI”. X-ray diffraction, 2 ligands (ZN, MG), 20 pockets (best druggability 0.89). MolNFT v1 #66391 on GenesisL1: 3D structure, binding sites…
- PDB
- 3HOY
- Type
- protein + DNA + RNA
- Length
- 3,952 residues
- Chains
- 15
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA-directed RNA polymerase II subunit RPB1; DNA-directed RNA polymerase II subunit RPB2…
- EC
- 2.7.7.6
- UniProt
- P04050, P08518, P16370, P20433, P20434, P20435, P34087, P20436, P27999, P22139, P38902, P40422
- Ligands
- ZN, MG
- Pockets
- 20 · best druggability 0.89
Structure
x-ray diffraction · 15 distinct chains · 31% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed RNA polymerase II subunit RPB1 (EC 2.7.7.6) | protein | 1419 | 40% helix, 15% strand | P04050 |
| B | DNA-directed RNA polymerase II subunit RPB2 (EC 2.7.7.6) | protein | 1105 | 28% helix, 20% strand | P08518 |
| C | DNA-directed RNA polymerase II subunit RPB3 (EC 2.7.7.6) | protein | 266 | 24% helix, 21% strand | P16370 |
| D | DNA-directed RNA polymerase II subunit RPB4 (EC 2.7.7.6) | protein | 178 | 49% helix, 5% strand | P20433 |
| E | DNA-directed RNA polymerases I, II, and III subunit RPABC1 (EC 2.7.7.6) | protein | 213 | 34% helix, 21% strand | P20434 |
| F | DNA-directed RNA polymerases I, II, and III subunit RPABC2 (EC 2.7.7.6) | protein | 87 | 29% helix, 16% strand | P20435 |
| G | DNA-directed RNA polymerase II subunit RPB7 (EC 2.7.7.6) | protein | 171 | 12% helix, 48% strand | P34087 |
| H | DNA-directed RNA polymerases I, II, and III subunit RPABC3 (EC 2.7.7.6) | protein | 133 | 2% helix, 33% strand | P20436 |
| I | DNA-directed RNA polymerase II subunit RPB9 (EC 2.7.7.6) | protein | 119 | 3% helix, 24% strand | P27999 |
| J | DNA-directed RNA polymerases I, II, and III subunit RPABC5 (EC 2.7.7.6) | protein | 65 | 48% helix, 2% strand | P22139 |
| K | DNA-directed RNA polymerase II subunit RPB11 (EC 2.7.7.6) | protein | 114 | 38% helix, 22% strand | P38902 |
| L | DNA-directed RNA polymerases I, II, and III subunit RPABC4 (EC 2.7.7.6) | protein | 46 | 0% helix, 11% strand | P40422 |
| T | 5'- D(*CP*CP*AP*AP*GP*CP*TP*CP*AP*AP*G*TP*AP*CP*TP*TP*AP*CP*GP* CP*CP*(BRU)P*GP*GP*TP*CP*AP*TP*TP*AP*CP*TP*AP*GP*TP*AP*CP*T P*GP*CP*C)-3' | dna | 19 | — | — |
| N | 5'- D(*CP*CP*GP*GP*CP*AP*GP*TP*AP*CP*TP*AP*GP*TP*AP*AP*AP*CP*TP *AP*GP*TP*AP*TP*T*GP*AP*AP*AP*GP*TP*AP*CP*TP*TP*GP*AP*GP*CP *TP*T)-3' | dna | 7 | — | — |
| P | 5'- R(*UP*AP*UP*AP*UP*GP*CP*A*UP*AP*AP*AP*GP*AP*CP*CP*AP*GP*GP* a)-3' | rna | 10 | — | — |
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 | 1017 | 0.89 | 0.91 | 118 | empty |
| 2 | 1060 | 0.87 | 0.88 | 121 | empty |
| 3 | 1097 | 0.87 | 0.88 | 129 | empty |
| 4 | 617 | 0.82 | 0.87 | 82 | empty |
| 5 | 1183 | 0.82 | 0.83 | 127 | empty |
Interfaces
37 interfaces between chains.
- A–B · 9622 Ų buried · 151 hydrogen bonds · protein-protein
- D–G · 2282 Ų buried · 23 hydrogen bonds · protein-protein
- A–E · 2173 Ų buried · 25 hydrogen bonds · protein-protein
- C–K · 2114 Ų buried · 15 hydrogen bonds · protein-protein
- A–F · 2045 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (nucleotide modification).
Compared structures
- 3HOY · Complete RNA polymerase II elongation complex VI · the same entry in another collection · chain T against T, 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 P20433
- Every structure of UniProt P20434
- Every structure of UniProt P20435
- Every structure of UniProt P34087
- 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 3HOY · PDBe 3HOY · UniProt P04050 · UniProt P08518 · UniProt P16370 · UniProt P20433 · UniProt P20434 · UniProt P20435 · UniProt P34087 · UniProt P20436 · UniProt P27999 · UniProt P22139 · UniProt P38902 · UniProt P40422
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