Research workbench
Bacteriophage N4 RNA polymerase II elongation complex 2
Analyse Bacteriophage N4 RNA polymerase II elongation complex 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DTA
- Type
- protein + DNA + RNA
- Length
- 672 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q8LTE4, Q8LTE3
- Ligands
- GTP, MG
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 250 | — | Q8LTE4 |
| B | — | protein | 404 | — | Q8LTE3 |
| C | — | dna | 11 | — | — |
| D | — | rna | 7 | — | — |
Ligands and binding sites
- GTP · Guanosine-5'-triphosphate · ligand · chains B, C, D
- MG · Magnesium ion · metal · 3 copies · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6DTA · Bacteriophage N4 RNA polymerase II elongation complex 2 · 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 Q8LTE4
- Every structure of UniProt Q8LTE3
- Elsewhere: RCSB PDB 6DTA · PDBe 6DTA · UniProt Q8LTE4 · UniProt Q8LTE3
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