Research workbench
Atomic structure of the poxvirus transcription late pre-initiation complex
Analyse Atomic structure of the poxvirus transcription late pre-initiation complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7AOF
- Type
- protein
- Length
- 4,034 residues
- Chains
- 9
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA-directed RNA polymerase 147 kda polypeptide; DNA-directed RNA polymerase…
- EC
- 2.7.7.6
- UniProt
- Q1PIV1, Q49PH2, Q49PG1, A4GDF1, Q49QC8, Q49PL6, Q1PIU7, Q49QI2, H2DZ00
- Ligands
- ZN, MG
- Pockets
- 20 · best druggability 0.88
Structure
electron microscopy · 9 distinct chains · 37% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed RNA polymerase 147 kda polypeptide (EC 2.7.7.6) | protein | 1268 | 42% helix, 16% strand | Q1PIV1 |
| B | DNA-directed RNA polymerase (EC 2.7.7.6) | protein | 1129 | 31% helix, 23% strand | Q49PH2 |
| C | DNA-directed RNA polymerase 35 kda subunit (EC 2.7.7.6) | protein | 304 | 38% helix, 22% strand | Q49PG1 |
| E | DNA-directed RNA polymerase subunit (EC 2.7.7.6) | protein | 184 | 24% helix, 24% strand | A4GDF1 |
| F | DNA-directed RNA polymerase 19 kda subunit (EC 2.7.7.6) | protein | 103 | 57% helix, 7% strand | Q49QC8 |
| G | DNA-directed RNA polymerase 18 kda subunit (EC 2.7.7.6) | protein | 153 | 12% helix, 52% strand | Q49PL6 |
| I | Protein H4 | protein | 665 | 42% helix, 13% strand | Q1PIU7 |
| J | DNA-directed RNA polymerase 7 kda subunit (EC 2.7.7.6) | protein | 61 | 36% helix, 8% strand | Q49QI2 |
| S | DNA-directed RNA polymerase 30 kda polypeptide (EC 2.7.7.6) | protein | 167 | 35% helix, 1% strand | H2DZ00 |
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 | 1124 | 0.88 | 0.90 | 140 | empty |
| 2 | 813 | 0.87 | 0.89 | 82 | empty |
| 3 | 656 | 0.86 | 0.90 | 84 | empty |
| 4 | 791 | 0.82 | 0.85 | 95 | empty |
| 5 | 998 | 0.79 | 0.81 | 74 | empty |
Interfaces
21 interfaces between chains.
- A–B · 9668 Ų buried · 113 hydrogen bonds · protein-protein
- B–I · 5447 Ų buried · 42 hydrogen bonds · protein-protein
- A–S · 4871 Ų buried · 44 hydrogen bonds · protein-protein
- A–I · 4176 Ų buried · 47 hydrogen bonds · protein-protein
- A–E · 2699 Ų buried · 30 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified, 1 disulfide (phosphorylation, disulfide).
Compared structures
- 7AOF · Atomic structure of the poxvirus transcription late pre-initiation complex · 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 Q1PIV1
- Every structure of UniProt Q49PH2
- Every structure of UniProt Q49PG1
- Every structure of UniProt A4GDF1
- Every structure of UniProt Q49QC8
- Every structure of UniProt Q49PL6
- Every structure of UniProt Q1PIU7
- Every structure of UniProt Q49QI2
- Every structure of UniProt H2DZ00
- Elsewhere: RCSB PDB 7AOF · PDBe 7AOF · UniProt Q1PIV1 · UniProt Q49PH2 · UniProt Q49PG1 · UniProt A4GDF1 · UniProt Q49QC8 · UniProt Q49PL6 · UniProt Q1PIU7 · UniProt Q49QI2 · UniProt H2DZ00
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