MolNFT v1 · #47189 · protein + DNA
Recognition of a DNA operator by the repressor of phage 434. a view at high resolution
2OR1 · DNA (5'- D(*AP*AP*GP*TP*AP*CP*AP*AP*AP*CP*TP*TP*TP*CP*TP*TP*…: “Recognition of a DNA operator by the repressor of phage 434. a view at high resolution”. X-ray diffraction, 1 pocket (best druggability 0.24). MolNFT v1 #47189 on…
- PDB
- 2OR1
- Type
- protein + DNA
- Length
- 166 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA (5'- D(*AP*AP*GP*TP*AP*CP*AP*AP*AP*CP*TP*TP*TP*CP*TP*TP*G P*TP*AP*T)-3'); DNA (5'…
- UniProt
- P16117
- Pockets
- 1 · best druggability 0.24
Structure
x-ray diffraction · 3 distinct chains · 68% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA (5'- D(*AP*AP*GP*TP*AP*CP*AP*AP*AP*CP*TP*TP*TP*CP*TP*TP*G P*TP*AP*T)-3') | dna | 20 | — | — |
| B | DNA (5'- D(*TP*AP*TP*AP*CP*AP*AP*GP*AP*AP*AP*GP*TP*TP*TP*GP*T P*AP*CP*T)-3') | dna | 20 | — | — |
| L, R | 434 repressor | protein | 63 | 68% helix, 0% strand | P16117 |
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 | 50 | 0.24 | 0.73 | 12 | empty |
Interfaces
6 interfaces between chains.
- A–B · 847 Ų buried · 81 hydrogen bonds · nucleic-nucleic
- A–L · 431 Ų buried · 4 hydrogen bonds · protein-nucleic
- A–R · 396 Ų buried · 7 hydrogen bonds · protein-nucleic
- B–L · 394 Ų buried · 5 hydrogen bonds · protein-nucleic
- B–R · 378 Ų buried · 6 hydrogen bonds · protein-nucleic
Compared structures
- 2OR1 · Recognition of a DNA operator by the repressor of phage 434. a view at high resolution · 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 P16117
- Elsewhere: RCSB PDB 2OR1 · PDBe 2OR1 · UniProt P16117
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