Research workbench
Transcription termination intermediate complex 1
Analyse Transcription termination intermediate complex 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6Z9P
- Type
- protein + DNA + RNA
- Length
- 6,518 residues
- Chains
- 16
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcription TERMINATION/ANTITERMINATION protein nusg; Transcription termination factor…
- EC
- 3.6.4.-, 2.7.7.6
- UniProt
- C3SID2, A0A0A0GPI6, C3SSN7, P0A7Z4, P0A800, P0A8V4, C3SIA2
- Ligands
- BEF, ADP, DG, MG, ZN
- Pockets
- 20 · best druggability 0.86
Structure
electron microscopy · 11 distinct chains · 33% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| G | Transcription TERMINATION/ANTITERMINATION protein nusg | protein | 112 | 31% helix, 9% strand | C3SID2 |
| a, b, c, d, e, f | Transcription termination factor rho (EC 3.6.4.-) | protein | 417 | 39% helix, 21% strand | A0A0A0GPI6 |
| A | Transcription TERMINATION/ANTITERMINATION protein nusa | protein | 495 | 36% helix, 15% strand | C3SSN7 |
| U | DNA-directed RNA polymerase subunit alpha (EC 2.7.7.6) | protein | 322 | 24% helix, 26% strand | P0A7Z4 |
| V | DNA-directed RNA polymerase subunit alpha (EC 2.7.7.6) | protein | 235 | 23% helix, 30% strand | P0A7Z4 |
| W | DNA-directed RNA polymerase subunit omega (EC 2.7.7.6) | protein | 79 | 66% helix, 0% strand | P0A800 |
| X | DNA-directed RNA polymerase subunit beta (EC 2.7.7.6) | protein | 1340 | 30% helix, 21% strand | P0A8V4 |
| Y | DNA-directed RNA polymerase subunit beta' (EC 2.7.7.6) | protein | 1358 | 34% helix, 16% strand | C3SIA2 |
| K | Non template strand | dna | 24 | — | — |
| L | Template strand | dna | 34 | — | — |
| R | Rut RNA | rna | 17 | — | — |
Ligands and binding sites
- BEF · Beryllium trifluoride ion · ligand · 5 copies · chains a, b, c, d, e, f
- ADP · Adenosine-5'-diphosphate · ligand · 5 copies · chains a, b, c, d, e, f
- DG · 2'-deoxyguanosine-5'-monophosphate · ligand · chains a, L
- MG · Magnesium ion · metal · 6 copies · chains a, b, c, d, e, f, Y, R
- ZN · Zinc ion · metal · 2 copies · chains Y
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 | 929 | 0.86 | 0.88 | 112 | empty |
| 2 | 874 | 0.84 | 0.86 | 77 | empty |
| 3 | 734 | 0.82 | 0.86 | 95 | empty |
| 4 | 1087 | 0.82 | 0.83 | 103 | empty |
| 5 | 1031 | 0.82 | 0.83 | 114 | empty |
Interfaces
42 interfaces between chains.
- X–Y · 8285 Ų buried · 87 hydrogen bonds · protein-protein
- U–V · 2408 Ų buried · 20 hydrogen bonds · protein-protein
- U–X · 1930 Ų buried · 18 hydrogen bonds · protein-protein
- d–e · 1871 Ų buried · 25 hydrogen bonds · protein-protein
- b–c · 1848 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 6Z9P · Transcription termination intermediate complex 1 · 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 C3SID2
- Every structure of UniProt A0A0A0GPI6
- Every structure of UniProt C3SSN7
- Every structure of UniProt P0A7Z4
- Every structure of UniProt P0A800
- Every structure of UniProt P0A8V4
- Every structure of UniProt C3SIA2
- Elsewhere: RCSB PDB 6Z9P · PDBe 6Z9P · UniProt C3SID2 · UniProt A0A0A0GPI6 · UniProt C3SSN7 · UniProt P0A7Z4 · UniProt P0A800 · UniProt P0A8V4 · UniProt C3SIA2
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