Research workbench
2-se-T2-DNA and native RNA hybrid in complex with RNase H catalytic domain D132N mutant
Analyse 2-se-T2-DNA and native RNA hybrid in complex with RNase H catalytic domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5US2
- Type
- protein + DNA + RNA
- Length
- 144 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9KEI9
- Ligands
- MG
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | — | rna | 6 | — | — |
| C | — | dna | 6 | — | — |
| A | — | protein | 132 | — | Q9KEI9 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5US2 · 2-Se-T2-DNA and native RNA hybrid in complex with RNase H catalytic domain D132N mutant · the same entry in another collection · chain B against B, TM-score 1.00
- Q9KEI9 · AlphaFold monomer V2.0 prediction for ribonuclease H (Q9KEI9) · a predicted model of the same protein · 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 Q9KEI9
- Elsewhere: RCSB PDB 5US2 · PDBe 5US2 · UniProt Q9KEI9
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