Research workbench
Crystal structure of fis bound to 27 bp optimal binding sequence F2
Analyse Crystal structure of fis bound to 27 bp optimal binding sequence F2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3JR9
- Type
- protein + DNA
- Length
- 243 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA-binding protein fis; DNA (27-mer)
- UniProt
- P0A6R3
- Pockets
- 4 · best druggability 0.63
Structure
x-ray diffraction · 4 distinct chains · 57% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-binding protein fis | protein | 91 | 58% helix, 11% strand | P0A6R3 |
| B | DNA-binding protein fis | protein | 98 | 56% helix, 10% strand | P0A6R3 |
| C | DNA (27-mer) | dna | 27 | — | — |
| D | DNA (27-mer) | dna | 27 | — | — |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 461 | 0.63 | 0.77 | 40 | empty |
| 2 | 159 | 0.43 | 0.74 | 22 | empty |
| 3 | 137 | 0.41 | 0.75 | 27 | empty |
| 4 | 79 | 0.35 | 0.76 | 16 | empty |
Interfaces
6 interfaces between chains.
- A–B · 2350 Ų buried · 22 hydrogen bonds · protein-protein
- C–D · 1165 Ų buried · 105 hydrogen bonds · nucleic-nucleic
- B–C · 287 Ų buried · 12 hydrogen bonds · protein-nucleic
- A–D · 281 Ų buried · 11 hydrogen bonds · protein-nucleic
- B–D · 267 Ų buried · 5 hydrogen bonds · protein-nucleic
Compared structures
- 3JR9 · Crystal structure of Fis bound to 27 bp optimal binding sequence F2 · the same entry in another collection · chain A against A, TM-score 1.00
- P0A6R3 · AlphaFold monomer V2.0 prediction for DNA-binding protein fis (P0A6R3) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 P0A6R3
- Elsewhere: RCSB PDB 3JR9 · PDBe 3JR9 · UniProt P0A6R3
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