Research workbench
Crystal structure of the P22 C2 repressor protein in complex with the synthetic operator 9T
Analyse Crystal structure of the P22 C2 repressor protein in complex with the synthetic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2R1J
- Type
- protein + DNA
- Length
- 172 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5'-D(*DCP*DAP*DTP*DTP*DTP*DAP*DAP*DGP*DAP*DTP*DAP*DTP*DCP*D…
- UniProt
- P69202
- Pockets
- 1 · best druggability 0.30
Structure
x-ray diffraction · 3 distinct chains · 67% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | 5'-D(*DCP*DAP*DTP*DTP*DTP*DAP*DAP*DGP*DAP*DTP*DAP*DTP*DCP*D TP*DTP*DAP*DAP*DAP*DTP*DA)-3' | dna | 20 | — | — |
| A | 5'-D(*DTP*DAP*DTP*DTP*DTP*DAP*DAP*DGP*DAP*DTP*DAP*DTP*DCP*D TP*DTP*DAP*DAP*DAP*DTP*DG)-3' | dna | 20 | — | — |
| L, R | Repressor protein C2 | protein | 66 | 67% helix, 2% strand | P69202 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 56 | 0.30 | 0.76 | 11 | empty |
Interfaces
6 interfaces between chains.
- B–A · 913 Ų buried · 70 hydrogen bonds · nucleic-nucleic
- L–R · 398 Ų buried · 5 hydrogen bonds · protein-protein
- B–R · 380 Ų buried · 7 hydrogen bonds · protein-nucleic
- A–L · 369 Ų buried · 7 hydrogen bonds · protein-nucleic
- B–L · 349 Ų buried · 8 hydrogen bonds · protein-nucleic
Compared structures
- 2R1J · Crystal Structure of the P22 c2 Repressor protein in complex with the synthetic operator… · the same entry in another collection · chain B against B, 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 P69202
- Elsewhere: RCSB PDB 2R1J · PDBe 2R1J · UniProt P69202
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