Research workbench
Crystal structure of spx in complex with the C-terminal domain of the RNA polymerase alpha subunit
Analyse Crystal structure of spx in complex with the C-terminal domain of the RNA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Z3E
- Type
- protein
- Length
- 186 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Regulatory protein spx; DNA-directed RNA polymerase alpha chain
- EC
- 2.7.7.6
- UniProt
- O31602, P20429
- Ligands
- SO4
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Regulatory protein spx | protein | 119 | 43% helix, 16% strand | O31602 |
| B | DNA-directed RNA polymerase alpha chain (EC 2.7.7.6) | protein | 67 | 58% helix, 4% strand | P20429 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 715 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1Z3E · Crystal Structure of Spx in Complex with the C-terminal Domain of the RNA Polymerase… · the same entry in another collection · chain A against A, TM-score 1.00
- P20429 · AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit alpha (P20429) · a predicted model of the same protein · chain B against A, TM-score 0.98
- O31602 · AlphaFold monomer V2.0 prediction for global transcriptional regulator spx (O31602) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 O31602
- Every structure of UniProt P20429
- Elsewhere: RCSB PDB 1Z3E · PDBe 1Z3E · UniProt O31602 · UniProt P20429
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