Research workbench
Crystal structure of escherichia COLI transcription-repair coupling factor
Analyse Crystal structure of escherichia COLI transcription-repair coupling factor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2EYQ
- Type
- protein
- Length
- 2,289 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcription-repair coupling factor
- UniProt
- P30958
- Ligands
- SO4
- Pockets
- 20 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcription-repair coupling factor | protein | 1146 | 41% helix, 18% strand | P30958 |
| B | Transcription-repair coupling factor | protein | 1143 | 38% helix, 17% strand | P30958 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 5 copies · chains A, B
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 | 1184 | 0.84 | 0.85 | 113 | EPE |
| 2 | 596 | 0.81 | 0.86 | 66 | empty |
| 3 | 962 | 0.77 | 0.80 | 94 | empty |
| 4 | 646 | 0.77 | 0.82 | 73 | SO4 |
| 5 | 1142 | 0.77 | 0.79 | 113 | EPE |
Interfaces
1 interface between chains.
- A–B · 1618 Ų buried · 38 hydrogen bonds · protein-protein
Compared structures
- 2EYQ · Crystal structure of Escherichia coli transcription-repair coupling factor · the same entry in another collection · chain A against A, TM-score 1.00
- P30958 · AlphaFold monomer V2.0 prediction for transcription-repair-coupling factor (P30958) · a predicted model of the same protein · chain B against A, TM-score 0.82
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 P30958
- Elsewhere: RCSB PDB 2EYQ · PDBe 2EYQ · UniProt P30958
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