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Crystal structure of soxr in complex with DNA
Analyse Crystal structure of soxr in complex with DNA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZHG
- Type
- protein + DNA
- Length
- 141 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Redox-sensitive transcriptional activator soxr; DNA (5'…
- UniProt
- P0ACS2
- Ligands
- FES
- Pockets
- 1 · best druggability 0.35
Structure
x-ray diffraction · 2 distinct chains · 61% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Redox-sensitive transcriptional activator soxr | protein | 121 | 61% helix, 5% strand | P0ACS2 |
| B | DNA (5'- D(*DGP*DCP*DCP*DTP*DCP*DAP*DAP*DGP*DTP*DTP*DAP*DAP*DCP*DTP*DTP*DGP*DA P*DGP*DGP*DC)-3') | dna | 20 | — | — |
Ligands and binding sites
- FES · Fe2/s2 (inorganic) cluster · ligand · chains A
- GOL · Glycerol · additive · chains A
- DTT · 2,3-dihydroxy-1,4-dithiobutane · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 84 | 0.35 | 0.75 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 299 Ų buried · 5 hydrogen bonds · protein-nucleic
Compared structures
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 P0ACS2
- Elsewhere: RCSB PDB 2ZHG · PDBe 2ZHG · UniProt P0ACS2
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